Publications

Department of Technical Biochemistry

All publications of the Department are listed here.

Publications

  1. 2022

    1. Royek, S., Bayer, M., Pfannstiel, J., Pleiss, J., Ingram, G., Stintzi, A., & Schaller, A. (2022). Processing of a plant peptide hormone precursor facilitated by post-translational tyrosine sulfation. Proc Natl Acad Sci USA, 119, e2201195119.
    2. Rapp, L., Marques, S., Nebel, B., Damborsky, J., & Hauer, B. (2022). Engineering CYP153A M.aq to Oxyfunctionalize its Inhibitor Dodecylamine Using a LC/MS Based Rapid Flow Analysis Screening. ChemCatChem.
    3. Zhang, H., Pérez-García, P., Dierkes, R., Danso, D., Pleiss, J., Almeida, A., Höcker, B., Schmitz-Streit, R., Chow, J., Streit, W., Applegate, V., Schumacher, J., Chibani, C., Sternagel, S., Preuss, L., Weigert, S., Schmeisser, C., Hallam, S., & Smits, S. (2022). The Bacteroidetes Aequorivita sp. and Kaistella jeonii produce promiscuous esterases with PET-hydrolyzing activity. Front Microbiol, 12, 803896. https://doi.org/10.3389/fmicb.2021.803896
    4. Mack, A., Emperle, M., Schnee, P., Pleiss, J., Bashtrykov, P., & Jeltsch, A. (2022). Preferential self-interaction of DNA methyltransferase DNMT3A subunits containing the R882H cancer mutation leads to dominant changes of flanking sequence preferences. J Mol Biol, 434, 167482.
  2. 2021

    1. Heinemann, P., Armbruster, D., & Hauer, B. (2021). Active-site loop variations adjust activity and selectivity of the cumene dioxygenase. Nature Communications, 12, 1095.
    2. Wissner, J., Schelle, J., Escobedo, W., Vogel, A., & Hauer, B. (2021). Semi‐Rational Engineering of Toluene Dioxygenase from Pseudomonas putida F1 towards Oxyfunctionalization of Bicyclic Aromatics. Advanced Synthesis & Catalysis, 363, 1–11.
    3. Bengel, L., Aberle, B., Egler-Kemmerer, A.-N., Kienzle, S., Hauer, B., & Hammer, S. (2021). Engineered enzymes enable selective N-alkylation of pyrazoles with simple haloalkanes. Angewandte Chemie International Edition, 60, 2–9.
    4. Henche, S., Nestl, B., & Hauer, B. (2021). Enzymatic Friedel-Crafts Alkylation Using Squalene-Hopene Cyclases. ChemCatChem.
    5. Orlando, M., Buchholz, P., Lotti, M., & Pleiss, J. (2021). The GH19 Engineering Database: sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19. PLoS One, 16, e0256817. https://doi.org/10.1371/journal.pone.0256817
    6. Buchholz, P., van, L. B., Eenink, B., Bornberg-Bauer, E., & Pleiss, J. (2021). Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation. J R Soc Interface, 18, 20210389. https://doi.org/10.1098/rsif.2021.0389
    7. Range, J., Halupczok, C., Lohmann, J., Swainston, N., Kettner, C., Bergmann, F., Weidemann, A., Wittig, U., Schnell, S., & Pleiss, J. (2021). EnzymeML – a data exchange format for biocatalysis and enzymology. FEBS J. https://doi.org/10.1111/febs.16318
    8. Schneider, A., Jegl, P., & Hauer, B. (2021). Stereoselective Directed Cationic Cascades Enabled by Molecular Anchoring in Terpene Cyclases. Angewandte Chemie International Edition, 60, 2–8.
    9. Pleiss, J. (2021). Standardized data, scalable documentation, sustainable storage –  EnzymeML as a basis for FAIR data management in biocatalysis. ChemCatChem, 13, 3909–3913. https://doi.org/10.1002/cctc.202100822
    10. Schatz, K., Franco-Moreno, J., Schäfer, M., Rose, A., Ferrario, V., Pleiss, J., Vazquez, P., Ertl, T., & Krone, M. (2021). Visual analysis of large-scale protein-ligand interaction data. Comput Graph Forum, 40, 394–408. https://doi.org/10.1111/cgf.14386
    11. Schatz, K., Friess, F., Schäfer, M., Buchholz, P., Pleiss, J., Ertl, T., & Krone, M. (2021). Analyzing the similarity of protein domains by clustering molecular surface maps. Comput Graph, 99, 114–127. https://doi.org/10.1016/j.cag.2021.06.007
    12. Hunold, A., Escobedo, W., Potoudis, E., Resende, D., Farr, T., Syrén, P., & Hauer, B. (2021). Assembly of a Rieske non-heme iron oxygenase multicomponent system from Phenylobacterium immobile E DSM 1986 enables pyrazon cis-dihydroxylation in E. coli. Applied Microbiology and Biotechnology, 105, 2003–20015.
    13. Stockinger, P., Borlinghaus, N., Sharma, M., Aberle, B., Grogan, G., Pleiss, J., & Nestl, B. (2021). Inverting the stereoselectivity of an NADH-dependent imine-reductase variant. ChemCatChem, 13, 5210–5215. https://doi.org/10.1002/cctc.202101057
    14. Carvalho, H., Ferrario, V., & Pleiss, J. (2021). The molecular mechanism of methanol inhibition in CALB-catalyzed alcoholysis: analyzing molecular dynamics simulations by a Markov state model. J Chem Theory Comput, 17, 6570–6582. https://doi.org/10.1021/acs.jctc.1c00559
    15. Faheem, M., Zhang, C., Morris, M., Pleiss, J., & Oelschlaeger, P. (2021). The role of synonymous mutations in the evolution of TEM β-lactamase genes. Antimicrob Agents Chemother, 65, e00018-21. https://doi.org/10.1128/AAC.00018-21
    16. Lohoff, C., Buchholz, P., Le, R.-H. M., & Pleiss, J. (2021). The Expansin Engineering Database: a navigation and classification tool for expansins and homologues. Proteins, 89, 149–162. https://doi.org/10.1002/prot.26001
    17. Rapp, L., Marques, S., Zukic, E., Rowlinson, B., Sharma, M., Grogan, G., Damborsky, J., & Hauer, B. (2021). Substrate Anchoring and Flexibility Reduction in CYP153AM.aq Leads to Highly Improved Efficiency toward Octanoic Acid. ACS Catalysis, 11, 3182–3189.
    18. Wissner, J., Escobedo, W., Vogel, A., & Hauer, B. (2021). An engineered toluene dioxygenase for a single step biocatalytical production of (-)-(1S,2R)-cis-1,2-dihydro-1,2-naphthalenediol. Journal of Biotechnology, 326, 37–39.
    19. Escobedo, W., Hammer, S., Wissner, J., & Hauer, B. (2021). Fast and easy synthesis of the non-commercially available standard isobutyl monophosphate (ammonium salt). MethodsX, 8, 101455.
    20. Escobedo, W., Wissner, J., & Hauer, B. (2021). A real-time 31 P-NMR-based approach for the assessment of glycerol kinase catalyzed monophosphorylations. MethodsX, 8.
    21. Farr, T., Wissner, J., & Hauer, B. (2021). A simple and efficient method for lyophilization of recombinant E. coli JM109 (DE3) whole-cells harboring active Rieske non-heme iron dioxygenases. MethodsX, 8.
  3. 2020

    1. Hauer, B. (2020). Embracing Nature’s Catalysts: A Viewpoint on the Future of Biocatalysis. ACS Catalysis, 10, 8418–8427.
    2. Gygli, G., & Pleiss, J. (2020). Simulation Foundry: automated and F.A.I.R. molecular modelling. J Chem Inf Model, 60, 1922–1927. https://doi.org/10.1021/acs.jcim.0c00018
    3. Mangiagalli, M., Carvalho, H., Natalello, A., Ferrario, V., Pennati, M., Barbiroli, A., Lotti, M., Pleiss, J., & Brocca, S. (2020). Diverse effects of aqueous polar co-solvents on Candida antarctica lipase B. Int J Biol Macromol, 150, 930–940. https://doi.org/10.1016/j.ijbiomac.2020.02.145
    4. Klenk, J., Ertl, J., Rapp, L., Fischer, M.-P., & Hauer, B. (2020). Expression and characterization of the benzoic acid hydroxylase CYP199A25 from Arthrobacter sp. Molecular Catalysis, 484.
    5. Stockinger, P., Schelle, L., Schober, B., Buchholz, P., Pleiss, J., & Nestl, B. (2020). Engineering of thermostable β-hydroxyacid dehydrogenase for asymmetric reduction of imines. ChemBioChem, 21, 3511–3514.
    6. Bauer, T., Buchholz, P., & Pleiss, J. (2020). The modular structure of α/β-hydrolases. FEBS J, 287, 1035–1053. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15071
    7. Eisenkolb, I., Jensch, A., Eisenkolb, K., Kramer, A., Buchholz, P., Pleiss, J., Spiess, A., & Radde, N. (2020). Modeling of biocatalytic reactions: A workflow for model calibration, selection and validation using Bayesian statistics. AIChE J, 66, e16866. https://doi.org/10.1002/aic.16866
    8. Rifai, E., Ferrario, V., Pleiss, J., & Geerke, D. (2020). A combined linear interaction energy and alchemical solvation free energy approach for protein-binding anity computation. J Chem Theory Comput, 16, 1300–1310.
    9. Gräff, M., Buchholz, P., Le Roes-Hill, M., & Pleiss, J. (2020). Multicopper oxidases: modular structure, sequence space and evolutionary relationships. Proteins.
    10. Stockinger, P., Roth, S., Müller, M., & Pleiss, J. (2020). Systematic evaluation of imine-reducing enzymes: Common principles in imine reductases, β-hydroxyacid dehydrogenases, and short-chain dehydrogenases/reductases. ChemBioChem, 21, 2689–2695. https://doi.org/10.1002/cbic.202000213
    11. Wissner, J., Ludwig, J., Escobedo, W., & Hauer, B. (2020). Strategy for identification of cis -dihydrodiendiol-degrading dehydrogenases in E. coli BW25113. MethodsX, 7, 101143.
    12. Wissner, J., Ludwig, L., Escobedo, W., & Hauer, B. (2020). An enhanced toluene dioxygenase platform for the production of cis-1,2-dihydrocatechol in Escherichia coli BW25113 lacking glycerol dehydrogenase activity. Journal of Biotechnology.
    13. Malzacher, S., Range, J., Halupczok, C., Pleiss, J., & Rother, D. (2020). BioCatHub, a graphical user interface for standardized data acquisition in biocatalysis. Chem Ing Tech, 92, 1251–1251.
    14. Al-Shameri, A., Petrich, M., Puring, K., Apfel, U., Nestl, B., & Lauterbach, L. (2020). Powering artificial enzymatic cascades with electrical energy. Angewandte Chemie International Edition, 59, 10929–10933.
    15. Wissner, J., Escobedo, W., Heinemann, P., Hunold, A., & Hauer, B. (2020). Methods for the detection and analysis of dioxygenase catalyzed dihydroxylation in mutant derived libraries. Methods in Enzymology, 1–31.
    16. Gygli, G., Xu, X., & Pleiss, J. (2020). Meta-analysis of viscosity of aqueous deep eutectic solvents and their components. Sci Rep, 10, 21395–21395. https://doi.org/10.1038/s41598-020-78101-y
    17. Roth, S., Stockinger, P., Steff, J., Steimle, S., Sautner, V., Tittmann, K., Pleiss, J., & Müller, M. (2020). Crossing the border: From keto- to imine reduction in short-chain dehydrogenases/reductases. ChemBioChem, 21, 2615–2619.
    18. Xu, X., Range, J., Gygli, G., & Pleiss, J. (2020). Analysis of thermophysical properties of deep eutectic solvents by data integration. J Chem Eng Data, 65, 1172–1179. https://doi.org/10.1021/acs.jced.9b00555
  4. 2019

    1. Buchholz, P., Ohs, R., Spieß, A., & Pleiss, J. (2019). Progress curve analysis within BioCatNet: comparing kinetic models for enzyme-catalyzed self-ligation. Biotechnol J, 14, e1800183.
    2. Gräff, M., Buchholz, P., Stockinger, P., Bommarius, B., Bommarius, A., & Pleiss, J. (2019). The Short-chain Dehydrogenase/Reductase Engineering Database (SDRED):  A classification and analysis system for a highly diverse enzyme family. Proteins, 87, 443–451.
    3. Gobeil, S., Ebert, M., Park, J., Gagné, D., Doucet, N., Berghuis, A., Pleiss, J., & Pelletier, J. (2019). The structural dynamics of engineered β-lactamases vary broadly on three timescales yet sustain native function. Sci Rep, 9, 6656–6656.
    4. Fries, A., Mazzaferro, L., Grüning, B., Bisel, P., Stibal, K., Buchholz, P., Pleiss, J., Sprenger, G., & Müller, M. (2019). Alteration of the route to menaquinone towards isochorismate - derived metabolites. ChemBioChem, 20, 1672–1677.
    5. Borlinghaus, N., Weinmann, L., Krimpzer, F., Scheller, P., Al-Shameri, A., Lauterbach, L., Coquel, A., & Lattemann, C. (2019). Cascade Biotransformation to Access 3-Methylpiperidine in Whole Cells. ChemCatChem, 11, 5738–5742.
    6. Schatz, K., Krone, M., Pleiss, J., & Ertl, T. (2019). Interactive visualization of biomolecules’ dynamic and complex properties. Eur Phys J Special Topics, 227, 1725–1739.
    7. Klaus, T., Seifert, A., Häbe, T., Nestl, B., & Hauer, B. (2019). An Enzyme Cascade Synthesis of Vanillin. Catalysts, 9.
    8. Bornscheuer, U., Hauer, B., Jaeger, K., & Schwaneberg, U. (2019). Directed Evolution Empowered Redesign of Natural Proteins for the Sustainable Production of Chemicals and Pharmaceuticals. Angewandte Chemie International Edition, 58, 36–40.
    9. Ferrario, V., & Pleiss, J. (2019). Molecular simulations of enzymes under non-natural conditions. Eur Phys J  Special Topics, 227, 1631–1638.
    10. Demming, R., Hammer, S., Nestl, B., Gergel, S., Fademrecht, S., Pleiss, J., & Hauer, B. (2019). Asymmetric Enzymatic Hydration of Unactivated, Aliphatic Alkenes. Angew Chem Int Ed Engl, 58, 173–177.
    11. Hinner, L., Wissner, J., Hauer, B., & Nebel, B. (2019). Efficient cellulose dissolution in a tertiary EHEMIM-EMIMOAc-water system. Journal of Molecular Liquids, 281, 236–242.
    12. Ferrario, V., Fischer, M., Zhu, Y., & Pleiss, J. (2019). Modelling of substrate access and substrate binding to cephalosporin acylases. Sci Rep, 9, 12402. https://doi.org/10.1038/s41598-019-48849-z
    13. Baz, J., Held, C., Pleiss, J., & Hansen, N. (2019). Thermophysical properties of glyceline-water mixtures investigated by molecular modelling. Phys Chem Chem Phys, 21, 6467–6476. https://doi.org/10.1039/C9CP00036D
    14. Al-Shameri, A., Borlinghaus, N., Weinmann, L., Scheller, P., Nestl, B., & Lauterbach, L. (2019). Synthesis of N-heterocycles from diamines via H2-driven NADPH recycling in the presence of O2. Green Chemistry, 21, 1396–1400.
    15. Buchholz, P., Ferrario, V., Pohl, M., Gardossi, L., & Pleiss, J. (2019). Navigating within thiamine diphosphate-dependent decarboxylases: Sequences, structures, functional positions, and binding sites. Proteins, 87, 774–785.
    16. Grüninger, M., Buchholz, P., Mordhorst, S., Strack, P., Müller, M., Hubrich, F., Pleiss, J., & Andexer, J. (2019). Chorismatases – the family is growing. Org Biomol Chem, 17, 2092–2098.
    17. Li, W., Jayakody, L., Franden, M., Wehrmann, M., Daun, T., Hauer, B., Blank, L., Beckham, G., Klebensberger, J., & Wierckx, N. (2019). Laboratory evolution reveals the metabolic and regulatory basis of ethylene glycol metabolism by Pseudomonas putida KT2440. Environmental Microbiology, 21, 3669–3682.
    18. Roddan, R., Gygli, G., Sula, A., Mendez-Sanchez, D., Pleiss, J., Ward, J., Keep, N., & Hailes, H. (2019). The acceptance and kinetic resolution of alpha-methyl substituted aldehydes by norcoclaurine synthases. ACS Catal, 9, 9640–9649. https://pubs.acs.org/doi/abs/10.1021/acscatal.9b02699
  5. 2018

    1. Wehrmann, M., & Klebensberger, J. (2018). Engineering thermal stability and solvent tolerance of the soluble quinoprotein PedE from P. putida KT2440 with a heterologous whole-cell screening approach. Microb Biotechnol, 11, 399–408.
    2. Halder, J., Nestl, B., & Hauer, B. (2018). Semi-Rational Engineering of the Naphthalene Dioxygenase from Pseudomonas sp. NCIB 9816-4 towards Selective Asymmetric Dihydroxylation. ChemCatChem, 10, 178–182.
    3. Kress, N., Halder, J., Rapp, L., & Hauer, B. (2018). Unlocked potential of dynamic elements in protein structures: channels and loops. Curr Opin Chem Biol, 47, 109–116.
    4. Facey, S., Nebel, B., Kontny, L., Allgaier, M., & Hauer, B. (2018). Rapid and complete degradation of diclofenac by native soil microorganisms. Environmental Technology & Innovation, 10, 55–61.
    5. Ferrario, V., Hansen, N., & Pleiss, J. (2018). Interpretation of cytochrome P450 monooxygenase kinetics by modeling of thermodynamic activity. J Inorg Biochem, 183, 172–178. https://doi.org/10.1016/j.jinorgbio.2018.02.016
    6. Borlinghaus, N., Gergel, S., & Nestl, B. (2018). Biocatalytic Access to Piperazines from Diamines and Dicarbonyls. ACS Catal, 8, 3727–3732.
    7. Darimont, D., Weissenborn, M., Nebel, B., & Hauer, B. (2018). Modulating proposed electron transfer pathways in P450BM3 led to improved activity and coupling efficiency. Bioelectrochemistry, 119, 119–123.
    8. Borlinghaus, N., & Nestl, B. (2018). Switching the cofactor specificity of an imine reductase. ChemCatChem, 10, 183–187.
    9. Lotti, M., Pleiss, J., Valero, F., & Ferrer, P. (2018). Enzymatic production of biodiesel: strategies to overcome methanol inactivation. Biotechnol J, 13, e1700155. https://doi.org/10.1002/biot.201700155
    10. Franden, M., Jayakody, L., Li, W., Wagner, N., Cleveland, N., Michener, W., Hauer, B., Blank, L., Wierckx, N., Klebensberger, J., & Beckham, G. (2018). Engineering Pseudomonas putida KT2440 for efficient ethylene glycol utilization. Metab Eng, 48, 197–207.
    11. Lenz, M., Fademrecht, S., Sharma, M., Pleiss, J., Grogan, G., & Nestl, B. (2018). New imine-reducing enzymes from beta-hydroxyacid dehydrogenases by single amino acid substitutions. Protein Engineering, Design and Selection, 31, 109–120.
    12. Klenk, J., Dubiel, P., Sharma, M., Grogan, G., & Hauer, B. (2018). Characterization and structure‐guided engineering of the novel versatile terpene monooxygenase CYP109Q5 from Chondromyces apiculatus DSM436. Microbial Biotechnology, 377–391.
    13. Demming, R., Fischer, M., Schmid, J., & Hauer, B. (2018). (De)hydratases-recent developments and future perspectives. Curr Opin Chem Biol, 43, 43–50.
    14. Ferrario, V., & Pleiss, J. (2018). Simulation of protein diffusion: a sensitive probe of protein-solvent interactions. J Biomol Struct Dyn, 37, 1534–1544.
    15. Buß, O., Buchholz, P., Gräff, M., Klausmann, P., Rudat, J., & Pleiss, J. (2018). The omega-Transaminase Engineering Database (oTAED): a navigation tool in protein sequence and structure space. Proteins, 86, 566–580.
    16. Martínez-Martínez, M., Coscolín, C., Santiago, G., Chow, J., Stogios, P., ..., Buchholz, P., Pleiss, J., ..., & Ferrer, M. (2018). Determinants and prediction of esterase substrate promiscuity patterns. ACS Chem Biol, 13, 225–234.
    17. Buchholz, P., Zeil, C., & Pleiss, J. (2018). The scale-free nature of protein sequence space. PLoS One, 13, e0200815.
    18. Baierl, A., Theorell, A., Mackfeld, U., Marquardt, P., Hoffmann, F., Moers, S., Nöh, K., Buchholz, P., Pleiss, J., & Pohl, M. (2018). Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase. ChemCatChem, 10, 2601–2611.
    19. Pleiss, J. (2018). Thermodynamic activity-based progress curve analysis in enzyme kinetics. Trends Biotechnol, 36, 234–238.
    20. Fernandes, A., Halder, J., Nestl, B., Hauer, B., Gernaey, K., & Krühne, U. (2018). Biocatalyst Screening with a Twist: Application of Oxygen Sensors Integrated in Microchannels for Screening Whole Cell Biocatalyst Variants. Bioengineering (Basel), 5(2), E30.
  6. 2017

    1. Klenk, J., Nebel, B., Porter, J., Kulig, J., Hussain, S., Richter, S., Tavanti, M., Turner, N., Hayes, M., & Hauer, B. (2017). The self-sufficient P450 RhF expressed in a whole cell system selectively catalyses the 5-hydroxylation of diclofenac. Biotechnol J., 12, 1600520.
    2. Benson, S., & Pleiss, J. (2017). Self-assembly nanostructures of triglyceride-water interfaces determine functional conformations of Candida antarctica lipase B. Langmuir, 33, 3151–3159.
    3. Zhang, Q., Catti, L., Pleiss, J., & Tiefenbacher, K. (2017). Terpene cyclizations inside a supramolecular catalyst: Leaving-group-controlled product selectivity and mechanistic studies. J Am Chem Soc, 139, 11482–11492.
    4. Kress, N., Rapp, J., & Hauer, B. (2017). Enantioselective Reduction of Citral Isomers in NCR Ene Reductase: Analysis of an Active-Site Mutant Library. ChemBioChem, 18, 717–720.
    5. Krone, M., Friess, F., Scharnowski, K., Reina, G., Fademrecht, S., Kulschewski, T., Pleiss, J., & Ertl, T. (2017). Molecular Surface Maps. IEEE Trans Vis Comput Graph, 23, 701–710.
    6. Lenz, M., Borlinghaus, N., Weinmann, L., & Nestl, B. (2017). Recent advances in imine reductase-catalzyed reactions. World J Microbiol Biotechnol, 33, 199.
    7. Buchholz, P., Fademrecht, S., & Pleiss, J. (2017). Percolation in protein sequence space. PLoS One, 12, e0189646.
    8. Nestl, B., Geinitz, C., Popa, S., Rizek, S., Haselbeck, R., Fischer, M., van, D. S., Culler, S., Grogan, G., & Hauer, B. (2017). Structural and functional insights into asymmetric enzymatic dehydration of alkenols. Nat Chem Biol, 13, 275–281.
    9. Demming, R., Otte, K., Nestl, B., & Hauer, B. (2017). Optimized Reaction Conditions Enable the Hydration of Non-natural Substrates by the Oleate Hydratase from Elizabethkingia meningoseptica. ChemCatChem, 9, 758–766.
    10. Schmid, J., Steiner, L., Fademrecht, S., Pleiss, J., Otte, K., & Hauer, B. (2017). Biocatalytic study of novel oleate hydratases. J Mol Catal B: Enzym, 133, S243–S249.
    11. Pleiss, J. (2017). Thermodynamic activity–based interpretation of enzyme kinetics. Trends Biotechnol, 35, 379–382.
    12. Lenz, M., Meisner, J., Quertinmont, L., Lutz, S., Kästner, J., & Nestl, B. (2017). Asymmetric Ketone Reduction by Imine Reductases. ChemBioChem, 18, 253–256.
    13. Wehrmann, M., Billard, P., Martin-Meriadec, A., Zegeye, A., & Klebensberger, J. (2017). Functional role of lanthanides in enzymatic activity and transcriptional regulation of PQQ-dependent alcohol dehydrogenases in Pseudomonas putida KT2440. MBIO, 8:e00570-17.
    14. Kühnel, L., Nestl, B., & Hauer, B. (2017). Enzymatic Addition of Alcohols to Terpenes by Squalene Hopene Cyclase Variants. ChemBioChem, 18, 2222–2225.
    15. Bastian, S., Hammer, S., Kress, N., Nestl, B., & Hauer, B. (2017). Enabling New Selectivities in the Cyclization of Citronellal by Squalene Hopene Cyclase Variants. ChemCatChem, 9, 4364–4368.
    16. Darimont, D., Weissenborn, M., Nebel, B., & Hauer, B. (2017). Modulating proposed electron transfer pathways in P450BM3 led to improved activity and coupling efficiency. Bioelectrochemistry, 119, 119–123.
    17. Otte, K., Maurer, E., Kirtz, M., Grabs, D., Althoff, E., Bartsch, S., Vogel, A., Nestl, B., & Hauer, B. (2017). Synthesis of sebacic acid using a de novo designed retro-aldolase as key catalyst. ChemCatChem, 9, 1378–1382.
  7. 2016

    1. Kulschewski, T., & Pleiss, J. (2016). Binding of solvent molecules to a protein surface in binary mixtures follows a competitive Langmuir model. Langmuir, 32, 8960–8968.
    2. Zeil, C., Widmann, M., Fademrecht, S., Vogel, C., & Pleiss, J. (2016). Microdiversity of TEM β-lactamases: a network analysis of sequence-function relationships and exploration of sequence space. Antimicrob Agents Chemother, 60, 2709–2717.
    3. Bock, S., Buchholz, P., Vogel, C., Holzapfel, A., Pleiss, J., Wiechert, W., Pohl, M., & Rother, D. (2016). Exploring the Sequence-Function Space of ThDP-Dependent Enzymes. Chemie Ingenieur Technik, 88, 1246.
    4. Benson, S., & Pleiss, J. (2016). Computational modeling of a biocatalyst at a hydrophobic substrate interface. In R. M. Nagel WE, Kröner DH (Ed.), High Performance Computing in Science and Engineering ´15. Springer International Publishing.
    5. Wetzl, D., Bolsinger, J., Nestl, B., & Hauer, B. (2016). α-Hydroxylation of Carboxylic Acids Catalyzed by Taurine Dioxygenase. ChemCatChem, 8, 1361–1366.
    6. Notonier, S., Gricman, L., Pleiss, J., & Hauer, B. (2016). Semi-rational protein engineering of CYP153A M.aq.-CPR BM3 for efficient terminal hydroxylation of short to long chain fatty acids. ChemBioChem, 17, 1550–1557.
    7. Alqarni, B., Colley, B., Klebensberger, J., McDougald, D., & Rice, S. (2016). Expression stability of 13 housekeeping genes during carbon starvation of Pseudomonas aeruginosa. J Microbiol Meth, 127, 182–187.
    8. Weissenborn, M., Notonier, S., Lang, S., Otte, K., Herter, S., Turner, N., Flitsch, S., & Hauer, B. (2016). Whole-cell microtiter plate screening assay for terminal hydroxylation of fatty acids by P450s. ChemCommun, 52, 6158–6161.
    9. Pleiss, J., & Zeil, C. (2016). Reply to The Curious Case of TEM-116. Antimicrob Agents Chemother, 60, 7001–7001.
    10. Weissenborn, M., Löw, S., Borlinghaus, N., Kuhn, M., Kummer, S., Rami, F., Plietker, B., & Hauer, B. (2016). Enzyme-Catalyzed Carbonyl Olefination by the E. coli Protein YfeX in the Absence of Phosphines. ChemCatChem.
    11. Schäfer, I., Lasko, G., Do, T., Pleiss, J., Weber, U., & Schmauder, S. (2016). Peptide–zinc oxide interaction: Finite element simulation using cohesive zone models based on molecular dynamics simulation. In S. I. Schmauder S (Ed.), Multiscale Materials Modeling. De Gruyter.
    12. Gricman, L., Weissenborn, M., Hoffmann, S., Borlinghaus, N., Hauer, B., & Pleiss, J. (2016). Redox Partner Interaction Sites in Cytochrome P450 Monooxygenases: In Silico Analysis and Experimental Validation. ChemistrySelect, 6, 1243–1251.
    13. Kirtz, M., Klebensberger, J., Otte, K., Richter, S., & Hauer, B. (2016). Production of ω-hydroxy octanoic acid with Escherichia coli. J Biotechnol, 230, 30–33.
    14. Buchholz, P., Vogel, C., Reusch, W., Pohl, M., Rother, D., Spieß, A., & Pleiss, J. (2016). BioCatNet: a database system for the integration of enzyme sequences and biocatalytic experiments. ChemBioChem, 17, 2093–2098.
    15. Jozwik, I., Kiss, F., Gricman, L., Abdulmughni, A., Brill, E., Zapp, J., Pleiss, J., Bernhardt, R., & Thunnissen, A. (2016). Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium. FEBS J, 283, 4128–4148.
    16. Widmann, M., & Pleiss, J. (2016). Sequence, structure, function: what we learn from analyzing protein families. In S. A (Ed.), Understanding enzymes. pan Standord Publishing.
    17. Eichler, A., Gricman, L., Herter, S., Kelly, P., Turner, N., Pleiss, J., & Flitsch, S. (2016). Enantioselective benzylic hydroxylation catalysed by P450 monooxygenases: characterisation of a P450cam mutant library and molecular modelling. ChemBioChem, 17, 426–432.
    18. Hoffmann, S., Weissenborn, M., Gricman, L., Notonier, S., Pleiss, J., & Hauer, B. (2016). The Impact of Linker Length on P450 Fusion Constructs: Activity, Stability and Coupling. ChemCatChem, 8, 1591–1597.
    19. Moghimian, P., Kilper, S., Srot, V., Rothenstein, D., Facey, SJ., Hauer, B., Bill, J., & van, A. PA. (2016). Phage-assisted assembly of organic–inorganic hybrid bilayers. International Journal of Materials Research.
    20. Syren, P., Henche, S., Eichler, A., Nestl, B., & Hauer, B. (2016). Squalene-hopene cyclases - evolution, dynamics and catalytic scope. Curr. Opin. Struct. Biol., 41, 73–82.
    21. Colley, B., Dederer, V., Carnell, M., Kjelleberg, S., Rice, S., & Klebensberger, J. (2016). SiaA/D interconnects c-di-GMP and RsmA signaling to coordinate cellular aggregation of Pseudomonas aeruginosa in response to environmental conditions. Front Microbiol, 7:179, doi: 10.3389/fmicb.2016.00179.
    22. Fademrecht, S., Scheller, P., Nestl, B., Hauer, B., & Pleiss, J. (2016). Identification of imine reductase-specific sequence motifs. Proteins, 84, 600–610.
    23. Reich, S., Nestl, B., & Hauer, B. (2016). Loop Grafted Old Yellow Enzymes in the Bienzymatic Cascade Reduction of Allylic Alcohols. ChemBioChem, 17, 561–565.
    24. Melcher, M., Facey, S., Henkes, T., Subkowski, T., & Hauer, B. (2016). Accelerated nucleation of hydroxyapatite using an engineered hydrophobin fusion protein. Biomacromolecules.
    25. Löw, S., Löw, I., Weissenborn, M., & Hauer, B. (2016). Enhanced Ene-Reductase Activity through Alteration of Artificial Nicotinamide Cofactor Substituents. ChemCatChem, 8, 911–915.
    26. Hoffmann, S., Danesh-Azari, H.-R., Spandolf, C., Weissenborn, M., Grogan, G., & Hauer, B. (2016). Structure-guided redesign of CYP153AM.aq. for the improved terminal hydroxylation of fatty acids. ChemCatChem, 8, 3234–3239.
    27. Hammer, S., Syren, P., & Hauer, B. (2016). Substrate Pre-Folding and Water Molecule Organization Matters for Terpene Cyclase Catalyzed Conversion of Unnatural Substrates. Chemistry Select, 1, 3589–3593.
    28. Hinner, L., Wissner, J., Beurer, A., Nebel, B., & Hauer, B. (2016). Homogeneous vinyl ester-based synthesis of different cellulose derivatives in 1-ethyl-3-methyl-imidazolium acetate. Green Chemistry.
    29. Lenz, M., Scheller, P., Richter, S., Hauer, B., & Nestl, B. (2016). Cultivation and purification of two stereoselective imine reductases from Streptosporangium roseum and Paenibacillus elgii. Protein Expr. Purif.
    30. Llaudet, E., Darimont, D., Samba, R., Matiychyn, I., Stelzle, M., Weissenborn, M., & Hauer, B. (2016). Expanding an Efficient, Electrically Driven and CNT-Tagged P450 System into the Third Dimension: A Nanowired CNT-Containing and Enzyme-Stabilising 3 D Sol-Gel Electrode. ChemBioChem, 17, 1367–1373.
  8. 2015

    1. Gricman, L., Vogel, C., & Pleiss, J. (2015). Identification of universal selectivity-determining positions in cytochrome P450 monooxygenases by systematic sequence-based literature mining. Proteins, 83, 1593-1603.
    2. Reznicek, O., Facey, SJ., & Hauer, B. (2015). Draft Genome Sequence of a Papaverine-Degrading, Gram-positive Arthrobacter sp., Isolated from Soil Near Hohenheim, Germany. Genome Announcements, 3, e00422-15.
    3. Steudle, A., Nestl, B., Hauer, B., & Stubenrauch, C. (2015). Activity of squalene-hopene cyclases in bicontinuous microemulsions. Colloids and Surfaces B: Biointerfaces, 135, 735–741.
    4. Hammer, S., Marjanovic, A., Dominicus, J., Nestl, B., & Hauer, B. (2015). Squalene Hopene Cyclases - Potency as Protonases for Stereoselective Brønsted Acid Catalysis. Nature Chemical Biology, 11, 121–126.
    5. Prins, A., Kleinsmidt, L., Khan, N., Kirby, B., Kudanga, T., Vollmer, J., Pleiss, J., Burton, S., & Le, R.-H. M. (2015). The effect of mutations near the T1 copper site on the biochemical characteristics of the small laccase from Streptomyces coelicolor A3(2). Enzyme Microb Technol, 68, 23–32.
    6. Simon, O., Klebensberger, J., Mückschel, B., Kleiber, I., Graf, N., Altenbuchner, J., Huber, A., Hauer, B., & Pfannstiel, J. (2015). Analysis of the molecular response of Pseudomonas putida KT2440 to the next-generation biofuel n-butanol. J Proteomics, 122, 11–25.
    7. Lotti, M., Pleiss, J., Valero, F., & Ferrer, P. (2015). Effects of methanol on lipases: molecular, kinetic and process issues in the production of biodiesel. Biotechnol J, 10, 22–30.
    8. Sasso, F., Kulschewski, T., Secundo, F., Lotti, M., & Pleiss, J. (2015). The effect of thermodynamic properties of solvent mixtures explains the difference between methanol and ethanol in C.antarctica lipase B catalyzed alcoholysis. J Biotechnol, 214, 1–8.
    9. Taudt, A., Arnold, A., & Pleiss, J. (2015). Simulation of protein association - Kinetic pathways towards crystal contacts. Phys Rev E, 91, 033311.
    10. Lonsdale, T., Lauterbach, L., Honda, M. S., Nestl, B., Hauer, B., & Lenz, O. (2015). H2-driven biotransformation of n-octane to Q1 1-octanol by Q2 a recombinant Pseudomonas putida strain co-synthesizing an O2-tolerant hydrogenase and a P450 monooxygenase. Chem. Commun., 51, 16173–16175.
    11. Reznicek, O., Luesken, F., Facey, SJ., & Hauer, B. (2015). Draft Genome Sequence of Phenylobacterium immobile Strain E (DSM 1986), Isolated from Uncontaminated Soil in Ecuador. Genome Announcements, 3, e00420-15.
    12. Lundemo, M., Notonier, S., Striedner, G., Hauer, B., & Woodley, J. (2015). Process limitations of a whole-cell P450 catalyzed reaction using a CYP153A-CPR fusion construct expressed in Escherichia coli. Appl. Microbiol. Biotechnol., 100, 1197–1208.
    13. Scheller, P., Lenz, M., Hammer, S., Hauer, B., & Nestl, B. (2015). Imine Reductase-Catalyzed Intermolecular Reductive Amination of Aldehydes and Ketones. ChemCatChem, 7, 3239–3242.
    14. Sandig, B., Michalek, L., Vlahovic, S., Antonovici, M., Hauer, B., & Buchmeiser, M. (2015). A Monolithic Hybrid Cellulose-2.5-Acetate/Polymer Bioreactor for Biocatalysis under Continuous Liquid-Liquid Conditions Using a Supported Ionic Liquid Phase. Chemistry, 21, 15835–15842.
    15. Felux, A.-K., Spiteller, D., Klebensberger, J., & Schleheck, D. (2015). Entner–Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc Natl Acad Sci U S A, 112, E4298–E4305.
    16. Löw, S., Nestl, B., Weissenborn, M., Zepeck, F., & Hauer, B. (2015). Process Investigations on the One-Pot Synthesis of Rifamycin S Avoiding Chlorinated Solvents. Org. Process Res. Dev., 19, 1544–1547.
    17. Reznicek, O., Facey, SJ., de, W. PP., Teunissen, AWRH., de, B. JAM., Nijland, JG., Driessen, AJM., & Hauer, B. (2015). Improved xylose uptake in Saccharomyces cerevisiae due to directed evolution of galactose permease Gal2 for sugar co-consumption. Journal of Applied Microbiology, 119, 99–111.
    18. Gally, C., Nestl, B., & Hauer, B. (2015). Engineering Rieske Non-Heme Iron Oxygenases for the Asymmetric Dihydroxylation of Alkenes. Angew. Chem. Int. Ed., 54, 12952–12956.
    19. Otte, K., & Hauer, B. (2015). Enzyme engineering in the context of novel pathways and products. Curr Opin Biotechnol, 35, 16–22.
  9. 2014

    1. Westphal, R., Vogel, C., Schmitz, C., Pleiss, J., Müller, M., Pohl, M., & Rother, D. (2014). A Tailor-Made Chimeric Thiamine Diphosphate Dependent Enzyme for the Direct Asymmetric Synthesis of (S)-Benzoins. Angew. Chem. Int. Ed., 53, 9376–9379.
    2. Widmann, M., & Pleiss, J. (2014). Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases. PLoS ONE, 9, e101813.
    3. Moghimian, P., Srot, V., Rothenstein, D., Facey, SJ., Harnau, L., Hauer, B., Bill, J., & van, A. PA. (2014). Adsorption and Self-Assembly of M13 Phage into Directionally Organized Structures on C and SiO2 Films. Langmuir, 30, 11428–11432.
    4. Reich, S., Kress, N., Nestl, B., & Hauer, B. (2014). Variations in the stability of NCR ene reductase by rational enzyme loop modulation. J. Struct. Biol., 185, 228–233.
    5. Scharnowski, K., Krone, M., Reina, G., Kulschewski, T., Pleiss, J., & Ertl, T. (2014). Comparative Visualization of Molecular Surfaces Using Deformable Models. Comput Graph Forum, 3, 191–200.
    6. Benson, S., & Pleiss, J. (2014). Molecular dynamics simulations of self-emulsifying drug delivery systems (SEDDS): influence of excipients on droplet nanostructure and drug localization. Langmuir, 30, 8471–8480.
    7. Scheller, P., Fademrecht, S., Hofelzer, S., Pleiss, J., Leipold, F., Turner, N., Nestl, B., & Hauer, B. (2014). Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases. ChemBioChem, 15, 2201–2204.
    8. Syren, P., Hammer, S., Classen, B., & Hauer, B. (2014). Entropy is Key to the Formation of Pentacyclic Terpenoids by Enzyme-Catalyzed Polycyclization. Angew. Chem. Int. Ed., 53, 4845–4849.
    9. Benson, S., & Pleiss, J. (2014). Solvent Flux Method (SFM): A case study of water access to Candida antarctica lipase B. J Chem Theory Comput, 10, 5206–5214.
    10. Pleiss, J. (2014). Systematic analysis of large enzyme families: identification of specificity- and selectivity-determining hotspots. ChemCatChem, 6, 944–950.
    11. Gricman, L., Vogel, C., & Pleiss, J. (2014). Conservation analysis of class-specific positions in cytochrome P450 monooxygenases: functional and structural relevance. Proteins, 82, 491–504.
    12. Ploss, M., Facey, SJ., Bruhn, C., Zemel, L., Hofmann, K., Stark, RW., Albert, B., & Hauer, B. (2014). Selection of peptides binding to metallic borides by screening M13 phage display libraries. BMC Biotechnology, 14, 12.
    13. Westphal, R., Jansen, S., Vogel, C., Pleiss, J., Müller, M., Rother, D., & Pohl, M. (2014). MenD from Bacillus subtilis: A Potent Catalyst for the Enantiocomplementary Asymmetric Synthesis of Functionalized α-Hydroxy Ketones. ChemCatChem, 6, 1082–1088.
    14. Schäfer, I., Lasko, G., Do, T., Pleiss, J., Weber, U., & Schmauder, S. (2014). Peptide - zinc oxide interaction: finite element simulation using cohesive zone models based on molecular dynamics simulation. Comp Mater Sci, 95, 320–327.
    15. Nestl, B., Hammer, S., Nebel, B., & Hauer, B. (2014). New Generation of Biocatalysts for Organic Synthesis. Angew. Chem. Int. Ed., 53, 3070–3095.
    16. Otte, K., Kittelberg, J., Kirtz, M., Nestl, B., & Hauer, B. (2014). Whole-Cell One-Pot Biosynthesis of Azelaic Acid. ChemCatChem, 6,4, 1003–1009.
    17. Subinya, M., Steudle, A., Nestl, B., Nebel, B., Hauer, B., Stubenrauch, C., & Engelskirchen, S. (2014). Physico-chemical aspects of lipase B from Candida antarctica in bicontinuous microemulstions. Langmuir, 30, 2993–3000.
    18. Nestl, B., & Hauer, B. (2014). Engineering of Flexible Loops in Enzymes. ACS Catalysis, 4, 3201–3211.
    19. Bogazkaya, A., von, B. C., Kriening, S., Busch, A., Seifert, A., Pleiss, J., Laschat, S., & Urlacher, V. (2014). Selective allylic hydroxylation of acyclic terpenoids by CYP154E1 from Thermobifida fusca YX. Beilstein J. Org. Chem, 10, 1347–1353.
    20. Baier, J., Blumenstein, N., Preusker, J., Jeurgens, L., Welzel, U., Do, T., Pleiss, J., & Bill, J. (2014). The influence of ZnO-binding 12-mer peptides on bio-inspired ZnO formation. Cryst Eng Comm, 16, 5301–5307.
    21. Vogel, C., & Pleiss, J. (2014). The modular structure of ThDP-dependent enzymes. Proteins, 82, 2523–2537.
    22. Nebel, B., Scheps, D., Honda, M. S., Nestl, B., Breuer, M., Wagner, H., Breitscheidel, B., Kratz, D., & Hauer, B. (2014). Biooxidation of n-butane to 1-butanol by engineered P450 monooxygenase under increased pressure. Journal of Biotechnology, 191, 86–92.
  10. 2013

    1. Krone, M., Reina, G., Schulz, C., Kulschewski, T., Pleiss, J., & Ertl, T. (2013). Interactive Extraction and Tracking of Biomolecular Surface Features. Comput Graph Forum, 32, 331–340.
    2. Benson, S., & Pleiss, J. (2013). Incomplete mixing versus clathrate-like structures: a molecular view on hydrophobicity in methanol-water mixtures. J Mol Model, 19, 3427–3436.
    3. Hailes, H., Rother, D., Müller, M., Westphal, R., Ward, J., Pleiss, J., Vogel, C., & Pohl, M. (2013). Engineering stereoselectivity of ThDP-dependent enzymes. FEBS J, 280, 6374–6394.
    4. Seitz, M., Syren, P., Steiner, L., Klebensberger, J., Nestl, B., & Hauer, B. (2013). Synthesis of heterocyclic terpenoids by promiscuous squalene-hopene cyclases. ChemBioChem, 14, 436–439.
    5. Roduner, E., Kaim, W., Sarkar, B., Urlacher, V., Pleiss, J., Gläser, R., Einicke, W., Sprenger, G., & Beifuss, U. (2013). Selective catalytic oxidation of C–H bonds with molecular oxygen. ChemCatChem, 5, 82–112.
    6. Zhong, L., Hauer, B., & Rosche, B. (2013). Catalytic biofilms on structured packing for the production of glycolic acid. J. Microbiol. Biotechnol., 23, 195–204.
    7. Kulschewski, T., & Pleiss, J. (2013). A molecular dynamics study of liquid aliphatic alcohols: simulation of density and self-diffusion coefficient using a modified OPLS force field. Mol Simulat, 39, 754–767.
    8. Kulschewski, T., Sasso, F., Secundo, F., Lotti, M., & Pleiss, J. (2013). Molecular mechanism of deactivation of C. antarctica lipase B by methanol. J Biotechnol, 168, 462–469.
    9. Westphal, R., Waltzer, S., Mackfeld, U., Widmann, M., Pleiss, J., Beigi, M., Müller, M., Rother, D., & Pohl, M. (2013). (S)-Selective MenD variants from Escherichia coli provide access to new functionalized chiral 2-hydroxy ketones. Chem Commun, 49, 2061–2063.
    10. Scheps, D., Honda, M. S., Richter, S., Marisch, K., Nestl, B., & Hauer, B. (2013). Synthesis of omega-hydroxy dodecanoic acid based on an engineered CYP153A fusion construct. Microbial. Biotechnol., 6, 694–707.
    11. Rothenstein, D., Facey, S., Ploss, M., Hans, P., Melcher, M., Srot, V., von, A. P., Hauer, B., & Bill, J. (2013). Mineralisation of gold nanoparticles using tailored M13 phages. Bioinspired, Biomimetic and Nanobiomaterials.
    12. Hammer, S., Syren, P., Seitz, M., Nestl, B., & Hauer, B. (2013). Squalene hopene cyclases: highly promiscuous and evolable catalysts for stereoselective C-C and C-X bond formation. Curr. Opin. Chem. Biol., 17, 293–300.
    13. Hammer, S., Nestl, B., & Hauer, B. (2013). The slumbering synthesis potential in enzymes: how can it be awakened? BIOspektrum, 19, 574–576.
    14. Westphal, R., Hahn, D., Mackfeld, U., Waltzer, S., Beigi, M., Widmann, M., Vogel, C., Pleiss, J., Müller, M., & Pohl, M. (2013). Tailoring (S)-selectivity of MenD from Escherichia coli. ChemCatChem, 13, 3587–3594.
    15. Nestl, B., Nebel, B., & Hauer, B. (2013). Dirigent effects in biocatalysis. Protein Engineering Handbook, 3, 1–27.
    16. Nestl, B., & Hauer, B. (2013). Protein engineering: chemistry gets the assist. Nat. Chem. Bio., 9, 470–471.
    17. Vallon, T., Glemser, M., Honda, M. S., Scheps, D., Schmid, J., Siemann-Herzberg, M., Hauer, B., & Takors, R. (2013). Production of 1-octanol from n-octane by Pseudomonas putida KT2440. Chemie Ingenieur Technik, 85, 841–848.
    18. Kazenwadel, C., Klebensberger, J., Richter, S., Pfannstiel, J., Gerken, U., Pickel, B., Schaller, A., & Hauer, B. (2013). Optimized expression of the dirigent protein AtDIR6 in Pichia pastoris and impact of glycosylation on protein structure and function. Appl Microbiol Biotechnol, 97, 7215–7227.
    19. Otte, K., Kirtz, M., Nestl, B., & Hauer, B. (2013). Synthesis of 9-oxononanoic acid, a precursor for biopolymers. ChemSusChem, 6, 2149–2156.
  11. 2012

    1. Fademrecht, S., Juhl, P., Sirim, D., & Pleiss, J. (2012). The triterpene cyclase protein family: a systematic analysis. Proteins, 80, 2009–2019.
    2. Kulschewski, T., & Pleiss, J. (2012). Simulation of enzymes in organic solvents. In S. Lutz & U. Bornscheuer (Eds.), Protein engineering handbook, vol.3. Wiley-VCH.
    3. Reich, S., Höffken, H., Rosche, B., Nestl, B., & Hauer, B. (2012). Crystal structure determination and mutagenesis analysis of the ene reductase NCR. ChemBioChem, 13, 2400–2407.
    4. Seitz, M., Klebensberger, J., Siebenhaller, S., Breuer, M., Siedenburg, G., Jendrossek, D., & Hauer, B. (2012). Substrate specificity of a novel squalene-hopene cyclase from Zymomonas mobilis. J Mol Catal B: Enzym, 84, 72–77.
    5. Mückschel, B., Simon, O., Klebensberger, J., Graf, N., Rosche, B., Altenbuchner, J., Huber, A., & Hauer, B. (2012). Ethylene Glycol Metabolism of Pseudomonas putida. Appl Environ Microbiol, 78, 8531–8539.
    6. Gruber, C., & Pleiss, J. (2012). Lipase B from Candida antarctica binds to hydrophobic substrate-water interfaces via hydrophobic anchors surrounding the active site entrance. J Mol Catal B, 84, 48–54.
    7. Seifert, A., & Pleiss, J. (2012). Identification of selectivity determinants in CYP monooxygenases by modelling and systematic analysis of sequence and structure. Curr Drug Metab, 13, 197–202.
    8. Honda, M. S., Scheps, D., Kühnel, L., Venegas, E., Seifert, A., Nestl, B., & Hauer, B. (2012). Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids. Chem. Commun., 48, 5115–5117.
    9. Kazenwadel, C., Eiben, S., Maurer, S., Beuttler, H., Wetzl, D., Hauer, B., & Koschorreck, K. (2012). Thiol-functionalization of acrylic ester monomers catalyzed by immobilized Humicola insolens cutinase. Enzyme Microbiol. Technol., 51, 9–15.
    10. Siedenburg, G., Jendrossek, D., Breuer, M., Juhl, B., Pleiss, J., Seitz, M., Klebensberger, J., & Hauer, B. (2012). Activation-independent cyclization of monoterpenoids. Appl Environ Microbiol, 78, 1055–1062.
    11. Pickel, B., Pfannstiel, J., Steudle, A., Lehmann, A., Gerken, U., Pleiss, J., & Schaller, A. (2012). A model of dirigent proteins derived from structural and functional similarities with alleneoxide cyclase and lipocalins. FEBS J, 279, 1980–1993.
    12. Baier, J., Naumburg, T., Blumenstein, N., Jeurgens, L., Welzel, U., Do, T., Pleiss, J., & Bill, J. (2012). Bio-inspired mineralization of zinc oxide in presence of ZnO-binding peptides. Biointerface Res Appl Chem, 2, 380–391.
    13. Widmann, M., Pleiss, J., & Oelschlaeger, P. (2012). Systematic analysis of metallo-b-lactamases using an automated database. Antimicrob Agents Ch, 56, 3481–3491.
    14. Pleiss, J. (2012). Rational design of enzymes. In K. Drauz, H. Gröger, & O. May (Eds.), Enzyme catalysis in organic synthesis. Wiley-VCH.
    15. Huynh, T., McDougald, D., Klebensberger, J., Al, Q. B., Barraud, N., Rice, S., Kjelleberg, S., & Schleheck, D. (2012). Glucose Starvation-Induced Dispersal of Pseudomonas aeruginosa Biofilms Is cAMP and Energy Dependent. PLoS One, 7, e42874.
    16. Widmann, M., Pleiss, J., & Samland, A. (2012). Computational tools for rational protein engineering of aldolases. Comput Struct Biotechnol J, 2, e201209016–e201209016.
    17. Ferrario, V., Braiuca, P., Tessaro, P., Knapic, L., Gruber, C., Pleiss, J., Ebert, C., Eichhorn, E., & Gardossi, L. (2012). Elucidating the structural and conformational factors responsible for the activity and substrate specificity of alkanesulfonate monooxygenase. J Biomol Struct Dyn, 30, 74–88.
    18. Vogel, C., Widmann, M., Pohl, M., & Pleiss, J. (2012). A standard numbering scheme for thiamine diphosphate-dependent decarboxylases. BMC Biochemistry, 13, 24–24.
    19. Gruber, C., & Pleiss, J. (2012). Molecular modeling of lipase binding to a substrate-water interface. Methods Mol Biol, 861, 313–327.
    20. Hutt, M., Kulschewski, T., & Pleiss, J. (2012). Molecular modelling of the mass density of single proteins. J Biomol Struct Dyn, 30, 318–327.
    21. Hammer, S., Dominicus, J., Syren, P., Nestl, B., & Hauer, B. (2012). Stereoselective Friedel-Crafts alkylation catalyzed by squalene hopene cyclases. Tetrahedron, 68, 7624–7629.
  12. 2011

    1. Rother, D., Kolter, G., Gerhards, T., Berthold, C., Gauchenova, E., Knoll, M., Pleiss, J., Müller, M., Schneider, G., & Pohl, M. (2011). S-selective mixed carboligation by structure-based design of the pyruvate decarboxylase from Acetobacter pasteurianus. ChemCatChem, 3, 1587–1596.
    2. Lalli, M., Facey, S., & Hauer, B. (2011). Protein Containers—Promising Tools for the Future. ChemBioChem, 12, 1519–1521.
    3. Scheps, D., Honda, M. S., Hoffmann, H., Nestl, B., & Hauer, B. (2011). Regioselective w-hydroxylation of medium-chain n-alkanes and primary alcohols by CYP153 enzymes from Mycobacterium marinum and Polaromonas sp. strain JS666. Org. Biomol. Chem., 9, 6727–6733.
    4. Steudle, A., & Pleiss, J. (2011). Modelling of lysozyme binding to a cation exchange surface at atomic detail: the role of flexibility. Biophys.J., 100, 3016–3024.
    5. Pleiss, J. (2011). Protein design in metabolic engineering and synthetic biology. Curr.Opin.Biotech., 22, 1–7.
    6. Habeych, D., Juhl, P., Pleiss, J., Vanegas, D., Eggink, G., & Boeriu, C. (2011). Biocatalytic synthesis of polyesters from sugar-based building blocks using immobilized Candida antarctica lipase B. J Mol Catal B - Enzym, 71, 1–9.
    7. Seifert, A., Antonovici, M., Hauer, B., & Pleiss, J. (2011). An efficient route to selective bio-oxidation catalysts: an iterative approach comprising modeling, diversification, and screening, based on CYP102A1. ChemBioChem, 12, 1346–1351.
    8. Beuttler, H., Hoffmann, J., Jeske, M., Hauer, B., Schmid, R., Altenbuchner, J., & Urlacher, V. (2011). Biosynthesis of zeaxanthin in recombinant Pseudomonas putida. Appl.Microbiol.Biotechnol., 89, 11377–11347.
    9. Alissandrotos, A., Baudendistel, N., Hauer, B., Baldenius, K., Flitsch, S., & Halling, P. (2011). Biocompatible functionalisation of starch. Chem.Commun., 47, 683–685.
    10. Krone, M., Falk, M., Rehm, S., Pleiss, J., & Ertl, T. (2011). Interactive exploration of protein cavities. Comput Graph Forum, 30, 673–682.
    11. Weber, E., Seifert, A., Antonovici, M., Geinitz, C., Pleiss, J., & Urlacher, V. (2011). Screening of a minimal enriched P450 BM3 mutant library for hydroxylation of cyclic and acyclic alkanes. Chem.Commun., 47, 944–946.
    12. Nestl, B., Nebel, B., & Hauer, B. (2011). Recent progress in industrial biocatalysis. Curr. Opin. Chem. Biol, 15, 187–193.
    13. Sirim, D., Wagner, F., Wang, L., Schmid, R., & Pleiss, J. (2011). The Laccase  Engineering Database: a classification and analysis system for laccases and related multicopper oxidases. Database, bar006.
    14. Gruber, C., & Pleiss, J. (2011). Systematic benchmarking of large molecular dynamics simulations employing GROMACS on massive multiprocessing facilities. J.Comput.Chem., 32, 600–606.
  13. 2010

    1. Rehm, S., Trodler, P., & Pleiss, J. (2010). Solvent-induced lid opening in lipases: A molecular dynamics study. Protein Sci., 19, 2122–2130.
    2. Widmann, M., Juhl, P., & Pleiss, J. (2010). Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A. BMC Genomics, 11, 123.
    3. Juhl, P., Doderer, K., Hollmann, F., Thum, O., & Pleiss, J. (2010). Engineering of Candida antarctica lipase B forhydrolysis of bulky carboxylic acid esters. J Biotechnol, 150, 474–480.
    4. Thai, K., & Pleiss, J. (2010). SHV Lactamase Engineering Database: a reconciliation tool for SHV β-lactamases in public databases. BMC Genomics, 11, 563–563.
    5. Koschorreck, K., Kazenwadel, C., Schmid, R., & Hauer, B. (2010). Heterologous expression, characterization and site-directed mutagenesis of cutinase CUTAB1 from Alternaria brassicicola. Appl. Microbiol. Biotechnol., 87, 991–997.
    6. Schmid, R., & Urlacher, V. (2010). Engineering cytochrome P450 monooxygenase CYP 116B3 for high dealkylation activity. Biotechnol Lett.
    7. Widmann, M., Radloff, R., & Pleiss, J. (2010). The Thiamine diphosphate dependent Enzyme Engineering Database: A tool for the systematic analysis of sequence and structure relations. BMC Biochemistry, 11, 9–9.
    8. Li, X., Klebensberger, J., & Rosche, B. (2010). Effect of gcl, glcB and aceA disruption on glyoxylate conversion by P. putida JM37. J Microbiol Biotechnol, 20, 1006–1010.
    9. Güven, A., Fioroni, M., Hauer, B., & Schwaneberg, U. (2010). Molecular understanding of sterically controlled compound release through an engineered channel protein (FhuA). J. Nanotechnology, 8, 14.
    10. Mueller, N., Stueckler, C., Hauer, B., Baudendistel, N., Housden, H., Bruce, N., & Faber, K. (2010). The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes. Adv. Synth. Catal, 325, 387–394.
    11. Roepcke, C., Muench, S., Schulze, H., Bachmann, T., Schmid, R., & Hauer, B. (2010). Analysis of phosphothionate pesticides using a chloroperoxidase pretreatment and acetylcholonesterase biosensor detection. J.Agric.Food Chem., 58, 8748–8756.
    12. Liu, D., Trodler, P., Eiben, S., Koschorrek, K., Mueller, M., Pleiss, J., Maurer, S., Branneby, C., & Schmid, R. (2010). Rational Design of Pseudozyma antarctica Lipase B Yielding a General Esterification Catalyst. Chem. Bio. Chem., 11, 789–795.
    13. Fisch, F., Fleites, C., Delenne, M., Baudendistel, N., Hauer, B., Turkenburg, J., Hart, S., Bruce, N., & Grogan, G. (2010). A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate ot fumerate by maleate isomerase. J. Am. Chem. Soc., 132, 11455–11457.
    14. Trodler, P., Eiben, S., Koschorreck, K., Müller, M., Pleiss, J., Maurer, S., Branneby, C., & Schmid, R. (2010). Rational design of Pseudozyma antarctica lipase B yielding a general esterification catalyst. ChemBioChem, 11, 789–795.
    15. Widmann, M., Trodler, P., & Pleiss, J. (2010). The isoelectric region of proteins: a systematic analysis. PLoS One, 5, e10546–e10546.
    16. Weber, E., Sirim, D., Schreiber, T., Bejoy, T., Pleiss, J., Hunger, M., Gläser, R., & Urlacher, V. (2010). Immobilization of P450 BM-3 monooxygenase on mesoporous molecular sieves with differentpore diameters. J Mol Catal B, 64, 29–37.
    17. Gatti-Lafranconi, P., Natalello, A., Rehm, S., Doglia, S., Pleiss, J., & Lotti, M. (2010). Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation. J Mol Biol, 395, 155–166.
    18. Girhard, M., Klaus, T., Khatri, Y., Bernhardt, R., & Urlacher, V. (2010). Characterization of the versatile monooxygenase CYP109B1 from Bacillus subtilis. Appl Microbiol Biotechnol, 87, 595–607.
    19. Sirim, D., Widmann, M., Wagner, F., & Pleiss, J. (2010). Prediction and analysis of the modular structure of cytochrome P450 monooxygenases. BMC Struct Biol, 10, 34–34.
    20. Alissandrotos, A., Baudendistel, N., Flitsch, S., Hauer, B., & Halling, P. (2010). Lipase-catalysed acylation of starch and determination of the degree of substitution by methanolysis and GC. BMC Biotechnology, 10, 82.
    21. Syren, P., Lindgre, E., Hoeffken, H., Branneby, C., Maurer, S., Hauer, B., & Hult, K. (2010). Increased activity of enzymatic transacylation of acrylates through rational design of lipases. J Mol. Catal. B, 65, 3–10.
  14. 2009

    1. Knoll, M., Hamm, T., Wagner, F., Martinez, V., & Pleiss, J. (2009). The PHA Depolymerase Engineering Database: A systematic analysis tool for the diverse family of polyhydroxyalkanoate (PHA) depolymerases. BMC Bioinformatics, 10, 89.
    2. Seifert, A., Vomund, S., Grohmann, K., Kriening, S., Urlacher, V., Laschat, S., & Pleiss, J. (2009). Rational design of a minimal and highly enrichedCYP102A1 mutant library with improved regio-, stereo- and chemoselectivity. ChemBioChem, 10, 853–861.
    3. Barraud, N., Schleheck, D., Klebensberger, J., Webb, J., McDougald, D., Rice, S., & Kjelleberg, S. (2009). Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic di-GMP levels, and enhanced dispersal. J Bacteriol, 191, 7333–7342.
    4. Girhard, M., Machida, K., Itoh, M., Schmid, R., Arisawa, A., & Urlacher, V. (2009). Regioselective biooxidation of (+)-valencene by recombinant E. coli expressing CYP109B1 from Bacillus subtilis in a two-liquid-phase system. Microb Cell Fact, 8, 36–36.
    5. Schleheck, D., Barraud, N., Klebensberger, J., Webb, J., Hassett, D., Rice, S., & Kjelleberg, S. (2009). Pseudomonas aeruginosa PAO1 preferentially grows as aggregates in liquid batch cultures and disperses upon starvation. PLOS ONE.
    6. Seifert, A., & Pleiss, J. (2009). Identification of selectivity-determining residues in cytochrome P450 monooxygenases: a systematic analysis of the substrate recognition site 5. Proteins, 74, 1028–1035.
    7. Koschorreck, K., Schmid, R., & Urlacher, V. (2009). Improving the functional expression of a Bacillus licheniformis laccase by random and site-directed mutagenesis. BMC Biotechnol, 9, 12–12.
    8. Bös, F., & Pleiss, J. (2009). Multiple molecular dynamics simulations of TEMbeta-lactamase: Dynamics and water binding of the Omega-loop. Biophys J, 97, 2550–2558.
    9. Juhl, P., Trodler, P., Tyagi, S., & Pleiss, J. (2009). Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking. BMC Struct Biol, 9, 39.
    10. Thai, Q., Bös, F., & Pleiss, J. (2009). The Lactamase Engineering Database: a critical survey of TEM sequences in public databases. BMC Genomics, 10, 390.
    11. Trodler, P., Schmid, R., & Pleiss, J. (2009). Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase. BMC Struct Biol, 9, 38.
    12. Branco, R., Graber, M., Denis, V., & Pleiss, J. (2009). Molecular mechanism of the hydration of Candida antarctica lipase B in gas phase: water adsorption isotherms and molecular dynamics simulations. ChemBioChem, 10, 2913–2919.
    13. Sirim, D., Wagner, F., Lisitsa, A., & Pleiss, J. (2009). The Cytochrome P450 Engineering Database: integration of biochemical properties. BMC Biochemistry, 10, 27.
    14. Klebensberger, J., Birkenmaier, A., Geffers, R., Kjelleberg, S., & Philipp, B. (2009). SiaA and SiaD are essential for inducing autoaggregation as a specific response to detergent stress in Pseudomonas aeruginosa. Environ Microbiol, 11, 3073–3086.
    15. Chen, B., Huang, Y., Pleiss, J., & Lin, Z. (2009). Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase. Biochemistry, 48, 11496–11504.
    16. Dietrich, M., Schmid, R., Pleiss, J., & Urlacher, V. (2009). Altering the regioselectivity of the subterminal fatty acid hydroxylase P450 BM-3 towards gamma- and delta-positions. J Biotechnol, 139, 115–117.
    17. Rosche, B., Hauer, B., Schmid, A., & Bühler, K. (2009). Microbial biofilms: a concept for industrial catalysis? Trends Biotechnol., 27(11), 636–643.
  15. 2008

    1. Koschorreck, K., Richter, S., Ene, A., Roduner, E., Schmid, R., & Urlacher, V. (2008). Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids. Appl Microbiol Biotechnol, 79, 217–224.
    2. Widmann, M., Clairo, M., Dippon, J., & Pleiss, J. (2008). Analysis of the distribution of functionally relevant rare codons. BMC Genomics, 9, 207.
    3. Trodler, P., & Pleiss, J. (2008). Modeling structure and flexibility of Candida antarctica lipase B in organic solvents. BMC Struct Biol, 8, 9.
    4. Trodler, P., Nieveler, J., Rusnak, M., Schmid, R., & Pleiss, J. (2008). Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography. J Chromatogr A, 1179, 161–167.
    5. Gocke, D., Walter, L., Gauchenova, E., Kolter, G., Knoll, M., Berthold, C., Schneider, G., Pleiss, J., Müller, M., & Pohl, M. (2008). Rational protein design of ThDP-dependent enzymes: engineering stereoselectivity. ChemBioChem, 9, 406–412.
    6. Bös, F., & Pleiss, J. (2008). Conserved water molecules stabilize the omega-loop in class A beta-lactamases. Antimicrob Agents Chemother, 52, 1072–1079.
    7. Koschorreck, K., Richter, S., Swierczek, A., Beifuss, U., Schmid, R., & Urlacher, V. (2008). Comparative characterization of four laccases from Trametes versicolor concerning phenolic C-C coupling and oxidation of PAHs. Arch Biochem Biophys, 474, 213–219.
    8. Mei, L., Urlacher, V., & Schmid, R. (2008). Cytochrome P450 BM-3 evolved by random and saturation mutagenesis as an effective indole-hydroxylating catalyst. Appl Biochem Biotechnol, 1444, 27–36.
    9. Messerschmidt, S., Kolbe, A., Müller, D., Knoll, M., Pleiss, J., & Kontermann, R. (2008). Novel single-chain Fv′ formats for the generation of immunoliposomes by site-directed coupling. Bioconjugate Chem., 19, 362–369.
    10. Branco, R., Seifert, A., Budde, M., Urlacher, V., Ramos, M., & Pleiss, J. (2008). Anchoring effects in a wide binding pocket: The molecular basis of regioselectivity in engineered cytochrome P450 monooxygenase from B. megaterium. Proteins, 73, 597–607.
    11. Dietrich, M., Eiben, S., Asta, C., Pleiss, J., & Urlacher, V. (2008). Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 from Bacillus licheniformis. Appl Microbiol Biotechnol, 79, 931–940.
    12. Urlacher, V. (2008). Catalysis with Cytochrome P450 monooxygenases. In R. Anastas, P. T.Crabtree (Ed.), Handbook of Green Chemistry - Green Catalysis. Wiley-VCH.
    13. Bidmon, K., Grottel, S., Bös, F., Pleiss, J., & Ertl, T. (2008). Visual abstractions of solvent pathlines near protein cavities. Comput Graph Forum, 27, 935–942.
    14. Knoll, M., & Pleiss, J. (2008). The Medium-Chain Dehydrogenase/Reductase Engineering Database: A systematic analysis of a diverse protein family to understand sequence-structure-function relationship. Protein Sci, 17, 1689–1697.
    15. Dietrich, M., Schmid, R., Ouyang, P., & Urlacher, V. (2008). Identification and functional expression of a Delta9-fatty acid desaturase from Psychrobacter urativorans in Escherichia coli. Lipids, 43, 207–213.
  16. 2007

    1. Krause, P., Singer, E., Darley, P., Klebensberger, J., Groettrup, M., & Legler, D. (2007). Prostaglandin E2 is a key factor for monocyte-derived dendritic cell maturation: enhanced T cell stimulatory capacity despite IDO. J Leuk Biol, 82, 1106–1114.
    2. Pleiss, J. (2007). Human Cytochrome P450 Monooxygenases – a General Model of Substrate Specificity and Regioselectivity. In V. B. U. Rolf D. Schmid (Ed.), Modern Biooxidation:Enzymes, Reactions and Applications. Wiley-VCH.
    3. Romankiewicz, A., Busch, A., Laschat, S., Schmid, R., & Urlacher, V. (2007). Separation and dentification of oxidized terpenoids by thin-layer chromatograph. Anal Letters, 40(7), 1487-1495.
    4. Klein, K., Tatzel, S., Raimundo, S., Saussele, T., Hustert, E., Pleiss, J., Eichelbaum, M., & Zanger, U. (2007). A natural variant of the heme-bindingsignature (R441C) resulting in complete loss of the function of CYP2D6. Drug Metab Dispos, 35, 1247–1250.
    5. Eiben, S., Bartelmäs, H., & Urlacher, V. (2007). Construction of a thermostable cytochrome P450 chimera derived from self-sufficient mesophilic parents. Appl. Microbiol. Biotechnol., 75(5), 1055–1061.
    6. Lange, S., Richter, S., & Schmid, R. (2007). High-level expression of extracellular lipase Lip2 from Yarrowia lipolytica in Pichia pastoris and its purification and characterization. Protein Expr. Purif., 53, 255–263.
    7. Birkenmaier, A., Holert, J., Moeller, H., Friemel, A., Schoenenberger, R., Suter, M., Klebensberger, J., & Philipp, B. (2007). Biochemical and genetic investigation of initial reactions in aerobic degradation of the bile acid cholate in Pseudomonas sp. strain Chol1. J Bacteriol, 189, 7165–7173.
    8. Soliman, N., Knoll, M., Abdel-Fattah, Y., Schmid, R., & Lange, S. (2007). Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt. Process Biochem, 42, 1090–1100.
    9. Oelschlaeger, P., & Pleiss, J. (2007). Hydroxyl groups in the betabeta sandwich of metallo-beta-lactamases favor enzyme activity: Tyr218 and Ser262 pull down the lid. J Mol Biol, 366, 316–329.
    10. Watanabe, Y., Laschat, S., Budde, M., Affolter, O., Shimada, Y., & Urlacher, V. (2007). Oxidation of acyclic monoterpenes by P450 BM-3 monooxygenase: influence of the substrate E/Z-isomerism on enzyme chemo- and regioselectivity. Tetrahedron, 63, 9413–9422.
    11. Pfeffer, J., Freund, A., Bel-Rhlid, R., Hansen, C., Reuss, M., Schmid, R., & Maurer, S. (2007). Highly efficient enzymatic synthesis of 2-monoacylglycerides and structured lipids and their production on a technical scale. Lipids, 42, 947–953.
    12. Kühnel, K., Maurer, S., Galeyeva, Y., Frey, W., Laschat, S., & Urlacher, V. (2007). Hydroxylation of dodecanoic acid and (2R,4R,6R,8R)-tetramethyldecanol on a preparative scale using an NADH-dependent CYP102A1 mutant. Adv Synth Catal, 349 (8-9), 1451–1461.
    13. Fischer, M., Knoll, M., Sirim, D., Wagner, F., Funke, S., & Pleiss, J. (2007). The Cytochrome P450 Engineering Database: a navigation and prediction tool for the cytochrome P450 protein family. Bioinformatics, 23, 2015–2017.
    14. Klebensberger, J., Lautenschlager, K., Bressler, D., Wingender, J., & Philipp, B. (2007). Detergent induced cell aggregation in subpopulations of Pseudomonas aeruginosa as a pre adaptive survival strategy. Environ Microbiol, 9, 2247–2259.
    15. Pflug, S., Richter, S., & Urlacher, V. (2007). Development of a fed-batch process for the production of the cytochrome P450 monooxygenase CYP102A1 from Bacillus megaterium in Escherichia coli. J Biotechnol, 129(3), 481–488.
    16. Feenstra, K., Starikov, E., Urlacher, V., Commandeur, J., & Vermeulen, N. (2007). Combining substrate dynamics, binding statistics, and energy barriers to rationalize regioselective hydroxylation of octane and lauric acid by CYP102A1 and mutants. Protein Sci, 16(3), 420–431.
    17. Girhard, M., Schuster, S., Dietrich, M., Dürre, P., & Urlacher, V. (2007). Cytochrome P450 monooxygenase from Clostridium acetobutylicum: A new alpha-fatty acid hydroxylase. Biochem Biophys Res Commun, 362(1), 2007–2119.
  17. 2006

    1. Fischer, M., Thai, Q., Grieb, M., & Pleiss, J. (2006). DWARF - a data warehouse system for analyzing protein families. BMC Bioinformatics, 7, 495–495.
    2. Knoll, M., Müller, M., Pleiss, J., & Pohl, M. (2006). Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase. Chembiochem, 7, 1928–1934.
    3. Schmid, R., & Rusnak, M. (2006). Functional expression of Candida antarctica lipase B in the Escherichia coli cytoplasm-a screening system for a frequently used biocatalyst. Appl Microbiol Biotechnol, 72, 1024–1032.
    4. Tyagi, S., & Pleiss, J. (2006). Biochemical profiling in silico - Predicting substrate specificities of large enzyme families. J Biotechnol, 124, 108–116.
    5. Klebensberger, J., Fritz, E., Schink, B., & Philipp, B. (2006). Cell aggregation of Pseudomonas aeruginosa strain PAO1 as an energy dependent stress response during growth with sodium dodecyl sulphate. Arch Microbiol, 185, 417–427.
    6. Urlacher, V., & Eiben, S. (2006). Cytochrome P450 monooxygenases: perspectives for synthetic application. Trends Biotechnol, 24, 324–330.
    7. Richter, S., Nieveler, J., Schulze, H., Bachmann, T., & Schmid, R. (2006). High yield production of a recombinant Nippostrongylus brasiliensis acetylcholinesterase mutant in Pichia pastoris and its purification. Biotechnol Bioeng, 93, 1017–1022.
    8. Schmid, R., & Urlacher, V. (2006). Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319. Appl Microbiol Biotechnol, 72, 876–882.
    9. Waibel, M., Huber, N., Schulze, H., & Bachmann, T. (2006). Screen-printed bienzymatic sensor based on sol-gel immobilized Nippostrongylus brasiliensis acetylcholinesterase and a cytochrome P450 BM-3 (CYP102-A1) mutant. Biosens Bioelectron, 21, 1132–1140.
    10. Pleiss, J. (2006). The promise of synthetic biology. Appl Microbiol Biotechnol, 73, 735–739.
    11. Urlacher, V., Bell, S., & Wong, L. (2006). The bacterial cytochrome P450 monooxygenases: P450cam and P450 BM-3. In U. V. B. Schmid R.D. (Ed.), Modern Biooxidation: Enzyme, Reactions and Applications (pp. 99–122). Wiley-VCH.
    12. Schmid, R. (2006). Bio-Cluster und Start-ups - eine japanische Innovationsoffensive. Nachr Chem Tech Lab, 986–988.
    13. Bachmann, T., Leinberger, D., Schumacher, U., & Autenrieth, I. (2006). DNA-Chip für invasive Mykosen: Schnelle Analyse von Candida- und Aspergillus-Arten. Management Und Krankenhaus, 2, 21–21.
    14. Seifert, A., Tatzel, S., Schmid, R., & Pleiss, J. (2006). Multiple molecular dynamics simulations of human P450 monooxygenase CYP2C9: the molecular basis of substrate binding and regioselectivity toward warfarin. Proteins, 64, 147–155.
    15. Urlacher, V., & Schmid, R. (2006). Recent advances in oxygenase-catalyzed biotransformations. Curr Opin Chem Biol, 10, 156–161.
    16. Pfeffer, J., Richter, S., Nieveler, J., Hansen, C., Rhlid, R., Schmid, R., & Rusnak, M. (2006). High yield expression of Lipase A from Candida antarctica in the methylotrophic yeast Pichia pastoris and its purification and characterisation. Appl Microbiol Biotechnol, 72, 931–938.
    17. Shumyantseva, V., Bulko, T., Samenkova, N., Kuznetsova, G., Usanov, S., Schulze, H., Bachmann, T., Schmid, R., & Archakov, A. (2006). A new format of electrodes for the electrochemical reduction of cytochromes P450. J Inorg Biochem, 100, 1353–1357.
    18. Lentz, O., Feenstra, A., Habicher, T., Hauer, B., Schmid, R., & Urlacher, V. (2006). Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system. Chembiochem, 7, 345–350.
    19. Budde, M., Morr, M., Schmid, R., & Urlacher, V. (2006). Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium. Chembiochem, 7, 789–794.
    20. Urlacher, V., Makhsumkhanov, A., & Schmid, R. (2006). Biotransformation of ionones by engineered cytochrome P450 BM-3. Appl Microbiol Biotechnol, 70, 53–59.
    21. Momoi, K., Hofmann, U., Schmid, R., & Urlacher, V. (2006). Reconstitution of beta-carotene hydroxylase activity of thermostable CYP175A1 monooxygenase. Biochem Biophys Res Commun, 339, 331–336.
    22. Eiben, S., Kaysser, L., Maurer, S., Kuhnel, K., Urlacher, V., & Schmid, R. (2006). Preparative use of isolated CYP102 monooxygenases-a critical appraisal. J Biotechnol, 124, 662–669.
  18. 2005

    1. Karpushova, A., Brümmer, F., Barth, S., Lange, S., & Schmid, R. (2005). Cloning, recombinant expression and biochemical characterisation of novel esterases from Bacillus sp. associated with the marine sponge Aplysina aerophoba. Appl Microbiol Biotechnol, 67, 59–69.
    2. Maurer, S., & Schmid, R. (2005). Biocatalysis for the epoxidation and hydroxylation of fatty acids and fatty alcohols. In C. T. Hou (Ed.), Handbook of industrial biocatalysis, 2005 (pp. 1–46). CRC Press LLC.
    3. Leinberger, D., Schumacher, U., Autenrieth, I., & Bachmann, T. (2005). Development of a DNA microarray for the detection and identification of fungal pathogens involved in invasive mycoses. J Clin Microbiol, 43, 4943–4953.
    4. Mei, L., Urlacher, V., & Schmid, R. (2005). Cytochrome P450BM-3 mutants with improved catalytic properties of hydroxylating indole to indigo by error-prone PCR. Prog Biochem Biophys, 32, 630–635.
    5. Riepe, F., Tatzel, S., Sippell, W., Pleiss, J., & Krone, N. (2005). Congenital adrenal hyperplasia: the molecular basis of 21-hydroxylase deficiency in H-2(aw18) mice. Endocrinology, 146, 2563–2574.
    6. Rusnak, M., Nieveler, J., Schmid, R., & Petri, R. (2005). The putative lipase, AF1763, from Archaeoglobus fulgidusis a carboxylesterase with a very high pH optimum. Biotechnol Lett, 11, 743–748.
    7. Ogawa, J., Schmid, R., & Shimizu, S. (2005). Indole hydroxylation by bacterial cytochrome P450 BM-3 and modulation of activity by cumene hydroperoxide. Biosci Biotechnol Biochem, 69, 293–300.
    8. Sulistyaningdyah, W., Ogawa, J., Maeda, C., Yano, Y., Schmid, R., & Shimizu, S. (2005). Hydroxylation activity of P450 BM-3 mutant F87V towards aromatic compounds and its application to the synthesis of hydroquinone derivatives from phenolic compounds. Appl Microbiol Biotechnol, 67, 556–562.
    9. Appel, D., Schmid, R., Dragan, C., Bureik, M., & Urlacher, V. (2005). A fluorimetric assay for cortisol. Anal Bioanal Chem, 383, 182–186.
    10. Bachmann, T., Grimm, V., Susa, M., & Knabbe, C. (2005). DNA-Microarrays, Schneller Nachweis von ESBL verursachenden Laktamasen. Management Und Krankenhaus, 3, 26–26.
    11. Dietrich, M., Grundmann, L., Kurr, K., Valinotto, L., Saussele, T., Schmid, R., & Lange, S. (2005). Recombinant production of human microsomal cytochrome P450 2D6 in the methylotrophic yeast Pichia pastoris. Chembiochem, 6, 2014–2022.
    12. Koschorreck, M., Fischer, M., Barth, S., & Pleiss, J. (2005). How to find soluble proteins: a comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli. BMC Genomics, 6, 1–10.
    13. Oelschlaeger, P., Mayo, S., & Pleiss, J. (2005). Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance. Protein Sci, 14, 765–774.
    14. Schuster, S., Enzelberger, M., Trauthwein, H., Schmid, R., & Urlacher, V. (2005). pHluorin-based in vivo assay for hydrolase screening. Anal Chem, 77, 2727–2732.
    15. Villatte, F., Kim, B., & Schmid, R. (2005). In-gel patch electrophoresis: a new method for environmental DNA purification. Electrophoresis, 26, 3055–3061.
    16. Bornscheuer, U., Henke, E., & Pleiss, J. (2005). Enzymatic methods. In A. Christoffers, J.; Baro (Ed.), Quaternary Stereocenters (pp. 315–327). Wiley-VCH.
    17. Maurer, S., Kühnel, K., Kaysser, L., Eiben, S., Schmid, R., & Urlacher, V. (2005). Catalytic hydroxylation in biphasic systems using CYP102A1 (P450 BM-3) mutants. Adv Synth Catal, 347, 1090–1098.
    18. Zhang, Y., Muench, S., Schulze, H., Perz, R., Yang, B., Schmid, R., & Bachmann, T. (2005). Disposable biosensor test for organophosphate and carbamate insecticides in milk. J Agric Food Chem, 29, 5110–5115.
    19. Schmid, R. (2005). BioEngineering in China. Transkript, 10, 81–83.
    20. Villatte, F., Schulze, H., Schmid, R., & Bachmann, T. (2005). Use of acetylcholinesterase and its modifications for biosensoring. In S. Parveen, M.; Kumar (Ed.), Recent Trends in the Acetylcholinesterase System (pp. 189–205). IOS Press.
    21. Schulze, H., Muench, S., Villatte, F., Schmid, R., & Bachmann, T. (2005). Highly sensitive insecticide detection through protein engineering of Nippostrongylus brasiliensis acetylcholinesterase B. Anal Chem, 77, 5823–5830.
  19. 2004

    1. Schulze, H., Nonhoff, U., Villatte, F., Schmid, R., & Bachmann, T. (2004). Highly sensitive neurotoxin detection using disposable acetylcholinesterase biosensors at elevated temperatures. Sensor Letters, 2, 121–124.
    2. Lentz, O., Urlacher, V., & Schmid, R. (2004). Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis. J Biotechnol, 108, 41–49.
    3. Blasco, F., Kauffmann, I., & Schmid, R. (2004). CYP175A1 from Thermus thermophilus HB27, the first beta-carotene hydroxylase of the P450 superfamily. Appl Microbiol Biotechnol, 64, 671–674.
    4. Tejo, B., Salleh, A., & Pleiss, J. (2004). Structure and dynamics of Candida rugosa lipase: the role of organic solvent. J Mol Model, 10, 358–366.
    5. Kauffmann, I., Schmitt, J., & Schmid, R. (2004). DNA isolation from soil samples for cloning in different hosts. Appl Microbiol Biotechnol, 64, 665–670.
    6. Schmid, R., Pleiss, J., & Urlacher, V. (2004). Biokatalyse: Selektivoxidation von C-H-Bindungen mit O2. Nachr Chem, 52, 767–772.
    7. Barth, S., Fischer, M., Schmid, R., & Pleiss, J. (2004). The database of epoxide hydrolases andhaloalkane dehalogenases: one structure, manyfunctions. Bioinformatics, 20, 2845–2847.
    8. Strohmeier, M., Hrmova, M., Fischer, M., Harvey, A., Fincher, G., & Pleiss, J. (2004). Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae. Protein Sci, 13, 3200–3213.
    9. Schulze, H., Schmid, R., & Bachmann, T. (2004). Activation of phosphorothionate pesticides based on a cytochrome P450 BM-3 (CYP102 A1) mutant for expanded neurotoxin detection in food using acetylcholinesterase biosensors. Anal Chem, 76, 1720–1725.
    10. Currle-Linde, N., Boes, F., Lindner, P., Pleiss, J., & Resch, M. (2004). A Management System for Complex Parameter Studies and Experiments in Grid Computing. In T. Gonzales (Ed.), Proceedings of the 16th IASTED International Conference on PDCS - International Conference on Parallel and Distributed Computing and Systems (pp. 34–39). Acta press.
    11. Susa, M., Knabbe, C., Schmid, R., & Bachmann, T. (2004). Development and validation of a diagnostic DNA microarray to detect quinolone-resistant Escherichia coli among clinical isolates. J Clin Microbiol, 42, 4083–4091.
    12. Urlacher, V., & Schmid, R. (2004). Protein engineering of the cytochrome P450 monooxygenase from Bacillus megaterium. Methods Enzymol, 388, 208–224.
    13. Grimm, V., Ezaki, S., Susa, M., Knabbe, C., Schmid, R., & Bachmann, T. (2004). Use of DNA microarrays for rapid genotyping of TEM beta-lactamases that confer resistance. J Clin Microbiol, 42, 3766–3774.
    14. Urlacher, V., Lutz-Wahl, S., & Schmid, R. (2004). Microbial P450 enzymes in biotechnology. Appl Microbiol Biotechnol, 64, 317–325.
    15. Sulistyaningdyah, W., Ogawa, J., Shinkyo, R., Sakaki, T., Inouye, K., Schmid, R., & Shimizu, S. (2004). Metabolism of polychlorinated dibenzo-p-dioxins by cytochrome P450 BM-3 and its mutant. Biotechnol Lett, 26, 1857–1860.
    16. Richter, T., Muerdter, T., Heinkele, G., Pleiss, J., Tatzel, S., Schwab, M., Eichelbaum, U., & Zanger, M. (2004). Potent mechanism-based inhibition of human CYP2B6 by clopidogrel and ticlopidine. J Pharmacol Exp Ther, 303, 189–197.
    17. Doderer, K., & Schmid, R. (2004). Fluorometric assay for determining epoxide hydrolase activity. Biotechnol Lett, 26, 835–839.
    18. Budde, M., Maurer, S., Schmid, R., & Urlacher, V. (2004). Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis. Appl Microb Biotech, 66, 180–186.
    19. Barth, S., Fischer, M., Schmid, R., & Pleiss, J. (2004). Sequence and structure of epoxide hydrolases: a systematic analysis. Proteins, 55, 846–855.
  20. 2003

    1. Oelschlaeger, P., Schmid, R., & Pleiss, J. (2003). Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations. Protein Eng, 16, 341–350.
    2. Fleming, B., Tian, Y., Bell, S., Wong, L., Urlacher, V., & Hill, H. (2003). Redox properties of cytochrome P450BM3 measured by direct methods. Eur J Biochem, 270, 4082–4088.
    3. Schulze, H., Vorlova, S., Villatte, F., Bachmann, T., & Schmid, R. (2003). Design of acetylcholinesterases for biosensor applications. Biosens Bioelectron, 18, 201–209.
    4. Henke, E., Bornscheuer, U., Schmid, R., & Pleiss, J. (2003). A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases. ChemBioChem, 4, 485–493.
    5. Oelschlaeger, P., Schmid, R., & Pleiss, J. (2003). Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6. Biochemistry, 42, 8945–8956.
    6. Villatte, F., Schulze, H., Schmid, R., & Bachmann, T. (2003). A long insertion reverts the functional effect of a substitution in acetylcholinesterase. Protein Eng, 16, 463–465.
    7. Fischer, M., & Pleiss, J. (2003). The Lipase Engineering Database: a navigation and analysis tool for protein families. Nucleic Acids Res, 31, 319–321.
    8. Schmid, R., & Lian, M. (2003). Biowissenschaften in China. Nachr Chem, 51, 527–531.
    9. Yano, J., Blasco, F., Schmid, R., Henne, A., & Poulos, T. (2003). Preliminary characterization and crystal structure of a thermostable cytochrome P450 from thermus thermophilus. J Biol Chem, 278, 608–616.
    10. Schmid, R. (2003). Chinese Bio Today. Chinese Bio Today.Com.
    11. Bessler, C., Schmitt, J., Maurer, K., & Schmid, R. (2003). Directed evolution of a bacterial alpha-amylase: toward enhanced pH-performance and higher specific activity. Protein Sci, 12, 2141–2149.
    12. Oelschlaeger, P., Lange, S., Schmitt, J., Siemann, M., Reuss, M., & Schmid, R. (2003). Identification of factors impeding the production of a single-chain antibody fragment in Escherichia coli by comparing in vivo and in vitro expression. Appl Microbiol Biotechnol, 61, 123–132.
    13. Lich, N., Barth, F., Pleiss, J., & Hai, T. (2003). Homology modelling of alpha-amylase from Saccharomycopsis fibuligera with maltohexaose substrate. Vietnam Journal of Biotechnology, 1, 149–159.
    14. Doderer, K., Schmitt, J., Hauer, B., & Schmid, R. (2003). High-throughput screening for bacterial epoxide hydrolyase activity. Anal Biochem, 321, 131–134.
    15. Quyen, D. T., Schmidt-Dannert, C., & Schmid, R. (2003). High-level expression of a lipase from Bacillus thermocatenulatus BTL2 in Pichia pastoris and some properties of the recombinant lipase. Protein Expr Purif, 28, 102–110.
    16. Schmid, R. (2003). Pocket Guide to Biotechnology and Genetic Engineering. In R. D. Schmid (Ed.), Pocket Guide to Biotechnology and Genetic Engineering (pp. 1–360). Wiley VCH.
    17. Bachmann, T. (2003). Transforming cyanobacteria into bioreporters of biological relevance. Trends Biotechnol, 21, 247–249.
    18. Maurer, S., Schulze, H., Schmid, R., & Urlacher, V. (2003). Immobilisation of P450 BM-3 and an NADP+ cofactor recycling system: towards a technical appication of heme-containing monooxygenases i fine chemical synthesis. Adv Synth Catal, 345, 802–810.
  21. 2002

    1. Oelschlaeger, P., Srikant-Iyer, S., Lange, S., Schmitt, J., & Schmid, R. (2002). Fluorophor-linked immunosorbent assay: a time- and cost-saving method for the characterization of antibody fragments using a fusion protein of a single-chain antibody fragment and enhanced green fluorescent protein. Anal Biochem, 309, 27–34.
    2. Urlacher, V., & Schmid, R. (2002). Biotransformations using prokaryotic P450 monooxygenases. Curr Opin Biotechnol, 13, 557–564.
    3. Bathelt, C., Schmid, R., & Pleiss, J. (2002). Regioselectivity of CYP2B6: homology modeling, molecular dynamics simulation, docking. J Mol Model, 8, 327–335.
    4. Schulze, H., Scherbaum, E., Anastassiades, M., Vorlova, S., Schmid, R., & Bachmann, T. (2002). Development, validation, and application of an acetylcholinesterase-biosensor test for the direct detection of insecticide residues in infant food. Biosens Bioelectron, 17, 1095–1105.
    5. Shumyantseva, V., Bulko, T., Usanov, S., Schmid, R., Nicolini, C., & Archakov, A. (2002). Construction and characterization of bioelectrocatalytic sensors based on cytochromes P450. J Inorg Biochem, 87, 185–190.
    6. Kusharyoto, W., Pleiss, J., Bachmann, T., & Schmid, R. (2002). Mapping of a hapten-binding site: molecular modeling and site-directed mutagenesis study of an anti-atrazine antibody. Protein Eng, 15, 233–241.
    7. Gentner, C., Schmid, R., & Pleiss, J. (2002). Primary alcohols in a ring structure: quantifying enantioselectivity of Pseudomonas cepacia lipase by an in silico assay. Colloids Surf B Biointerfaces, 26, 57–66.
    8. Henke, E., Pleiss, J., & Bornscheuer, U. (2002). Activity of lipases and esterases towards tertiary alcohols: insights into structure-function relationships. Angew Chem Int Ed, 41, 3211–3213.
    9. Schulze, H., Schmid, R., & Bachmann, T. (2002). Rapid detection of neurotoxic insecticides in food using disposable acetyicholinesterase-biosensors and simple solvent extraction. Anal Bioanal Chem, 372, 268–272.
    10. Villatte, F., Schulze, H., Schmid, R., & Bachmann, T. (2002). A disposable acetylcholinesterase-based electrode biosensor to detect anatoxin-a(s) in water. Anal Bioanal Chem, 372, 322–326.
    11. Schmitt, J., Brocca, S., Schmid, R., & Pleiss, J. (2002). Blocking the tunnel: engineering of Candida rugosa lipase mutants with short chain length specificity. Protein Eng, 15, 595–601.
    12. Bornscheuer, U., & Schmid, R. (2002). Efficient water removal in lipase-catalyzed esterifications using a low-boiling-point azeotrope. Biotechnol Bioeng, 78, 31–34.
    13. Schlecht, U., Nomura, Y., Bachmann, T., & Karube, I. (2002). Reversible surface thiol immobilization of carboxyl group containing haptens to a BIAcore biosensor chip enabling repeated usage of a single sensor surface. Bioconjug Chem, 13, 188–193.
    14. Villatte, F., & Bachmann, T. (2002). How many genes encode cholinesterase in arthropods? Pesticide Biochem Physiol, 73, 122–129.
    15. Mbeunkui, F., Richaud, C., Etienne, A., Schmid, R., & Bachmann, T. (2002). Bioavailable nitrate detection in water by an immobilized luminescent cyanobacterial reporter strain. Appl Microbiol Biotechnol, 60, 306–312.
    16. Enzelberger, M., & Quake, S. (2002). A nanoliter rotary device for polymerase chain reaction. Electrophoresis, 23, 1531–1536.
    17. Vorlova, S., Bornscheuer, U., Gatfield, I., Hilmer, J., Bertram, H., & Schmid, R. (2002). Enantioselective Hydrolysis of d,l-Menthyl Benzoate to L-(-)-Menthol by Recombinant Candida rugosa Lipase LIP1. Adv Synth Catal, 344, 1152–1155.
    18. Shumyantseva, V., Bulko, T., Schmid, R., & Archakov, A. (2002). Photochemical properties of a riboflavins/cytochrome P450 2B4 complex. Biosens Bioelectron, 17, 233–238.
  22. 2001

    1. Kahlow, U., Schmid, R., & Pleiss, J. (2001). A model of the pressure dependence of the enantioselectivity of Candida rugosa lipase towards (±)-menthol. Protein Sci, 10, 1942–1952.
    2. Ivanov, Y., Kanaeva, I., Gnedenko, O., Pozdnev, V., Shumyantseva, V., Samenkova, N., Kznetsova, G., Tereza, A., & Schmid, R. (2001). Optical biosensor investigation of interactions of biomembrane and water-soluble cytochromes P450 and their redox partners with covalently immobilized phosphatidylethanolamine layers. J Mol Recognit, 14, 185–196.
    3. Traub, P., Schmidt-Dannert, C., Schmitt, J., & Schmid, R. (2001). Gene synthesis, expression in E. coli, and in vitro refolding of Pseudomonas sp. KWI 56 and Chromobacterium viscosum lipases and their chaperones. Appl Microbiol Biotechnol, 55, 198–204.
    4. Bornscheuer, U., Stadler, G., Lutz-Wahl, S., Otto, R., Reuss, M., & Schmid, R. (2001). Regioselective lipase-catalyzed synthesis of glucose ester on preparative scale. Eur J Lipid Sci Technol, 103, 583–587.
    5. Appel, D., Lutz-Wahl, S., Fischer, P., Schwaneberg, U., & Schmid, R. (2001). A P450 BM-3 mutant hydroxylates of alkanes, cycloalkanes, arenes and heteroarenes. J Biotechnology, 88, 167–171.
    6. Ogawa, J., Schmid, R., & Shimizu, S. (2001). Residue size at position 87 of cytochrome P450 BM-3 determines its stereoselectivity in propylbenzene and 3-chlorostyrene oxidation. FEBS Lett, 508, 249–252.
    7. Villatte, F., Bachmann, T., Hussein, A., & Schmid, R. (2001). Acetylcholinesterase assay for rapid expression screening in liquid and solid media. BioTechniques, 30, 81–86.
    8. Schreiter, P., Gillor, O., Post, A., Belkin, S., Schmid, R., & Bachmann, T. (2001). Monitoring of phosphorus bioavailability in water by an immobilized luminescent cyanobacterial reporter strain. Biosens Bioelectron, 16, 811–818.
    9. Lange, S., Schmitt, J., & Schmid, R. (2001). High-level expression of the recombinant, atrazine-specific Fab fragment K411B by the methylotrophic yeast Pichia pastoris. J Immunol Methods, 255, 103–114.
    10. Musidlowska, A., Lange, S., & Bornscheuer, U. (2001). Durch Überexpression in der Hefe Pichia pastoris zu erhöhter Enantioselektivität: neue Aspekte bei der Anwendung von Schweineleber-Esterase. Angew Chem Int Ed, 113, 2934–2936.
    11. Villatte, F., Bachmann, T., Hussein, A., & Schmid, R. (2001). Expression level of heterologous proteins in Pichia pastoris is influenced by flasks design. Appl Microbiol Biotechnol, 55, 463–465.
    12. Schulz, T., Schmid, R., & Pleiss, J. (2001). Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcohols. J Mol Model, 7, 265–270.
    13. Ogawa, J., Schmid, R., & Shimizu, S. (2001). Engineering cytochrome P450 BM-3 for oxidation of polycyclic aromatic hydrocarbons. Appl Environ Microbiol, 67, 5735–5739.
    14. Lentz, O., Schwaneberg, U., Lutz-Wahl, S., Fischer, P., & Schmid, R. (2001). Modification of the fatty acid specificity of cytochrome P450 BM-3 from Bacillus megaterium by directed evolution: a validated assay. J Mol Catal B Enzym, 15, 123–133.
    15. Minning, S., Serrano, A., Ferrer, P., Sola, C., Schmid, R., & Valero, F. (2001). Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastoris. J Biotechnol, 86, 59–70.
    16. Lange, S., Musidlowska, A., Schmidt-Dannert, C., Schmitt, J., & Bornscheuer, U. (2001). Cloning, functional expression, and characterization of recombinant pig liver esterase. ChemBioChem, 2, 576–582.
    17. Bachmann, T., Pleiss, J., Villatte, F., & Schmid, R. (2001). Bioresponse-Linked Analysis Based on Acetylcholinesterase Inhibition. In H. B (Ed.), Bioresponse-Linked Instrumental Analysis. B.G. Teubner.
    18. Liu, A., Somers, N., Kazlauskas, R., Brush, T., Zocher, F., Enzelberger, M., Bornscheuer, U., & Horsman, G. (2001). Mapping the substrate selectivity of new hydrolases using colorimetric screening: lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes. Biochimica et Biophysica Acta-Protein Structure and Molecular Enzymology; Tetrahedron Asymmetry, 12, 545–556.
    19. Musidlowska, A., Lange, S., & Bornscheuer, U. (2001). By overexpression in the yeast Pichia pastoris to enhanced enantioselectivity: New aspects in the application of pig liver esterase. Angew Chem Int Ed, 40, 2851–2853.
    20. Bornscheuer, U., Stadler, G., Lutz-Wahl, S., Reuss, M., & Schmid, R. (2001). Production of sugar fatty acid esters by enzymatic esterification in a stirred-tank membrane reactor: optimization of parameters by response surface methodology. J Am Oil Chem Soc, 78, 147–153.
    21. Schwaneberg, U., Fischer, M., Schmitt, J., Pleiss, J., Lutz-Wahl, S., & Schmid, R. (2001). Rational evolution of a medium chain-specific cytochrome P-450 BM-3 variant. Biochim Biophys Acta, 1545, 114–121.
    22. Baumeister, F., Konig, A., Schmid, R., Kretschmer, A., Bachmann, T., & Metzger, J. (2001). Biosensors watching over the nitrification at wastewater treatment plants. In Stuttgarter Berichte zur SiedlungswasserwirtschaftStickstoff im Wasser/Abwasser (pp. 175–185). Kommissionsverlag R. Oldenbourg.
  23. 2000

    1. Bornscheuer, U., Pleiss, J., Schmidt-Dannert, C., & Schmid, R. (2000). Lipases from Rhizopus species: genetics, structure and applications. In L. Alberghina (Ed.), Protein engineering in industrial biotechnology (pp. 115–134). CRC Press.
    2. Otto, R., Scheib, H., Bornscheuer, U., Pleiss, J., Syldatk, C., & Schmid, R. (2000). Substrate specificity of lipase B from Candida antarctica in the synthesis of arylaliphatic glycolipids. J Mol Catal B Enzym, 8, 201–211.
    3. Schwaneberg, U., Appel, D., Schmitt, J., & Schmid, R. (2000). P450 in biotechnology: zinc driven w-hydroxylation of p-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst. J Biotechnol, 84, 249–257.
    4. Peters, H., Schmidt-Dannert, C., Bornscheuer, U., & Schmid, R. (2000). Purification and reconstitution of an integral membrane protein, the photoreaction center of Rhodobacter sphaeroides, using synthetic sugar esters. BioTechniques, 28, 1214–1219.
    5. Shumyantseva, V., Bulko, T., Bachmann, T., Bilitewski, U., Schmid, R., & Archakov, A. (2000). Electrochemical reduction of flavocytochromes 2B4 and 1A2 and their catalytic activity. Arch Biochem Biophys, 377, 43–48.
    6. Kovac, A., Scheib, H., Pleiss, J., Schmid, R., & Paltauf, F. (2000). Molecular basis of lipase stereoselectivity. Eur J Lipid Sci Tech, 102, 61–77.
    7. Pleiss, J., Fischer, M., Peiker, M., Thiele, C., & Schmid, R. (2000). Lipase Engineering Database: understanding and exploiting sequence-structure-function relationships. J Mol Catal B: Enzym, 10, 491–508.
    8. Pleiss, J., Fischer, M., Scheib, H., Schulz, T., & Schmid, R. (2000). Modelling structure-function relationship of lipase binding sites-a case study of specificity and selectivity. In G. Kokotos (Ed.), Lipases and LipidsStructure, function and biotechnological applications (pp. 21–39). Crete University Press.
    9. Köhler, S., Belkin, S., & Schmid, R. (2000). Reporter gene bioassays in environmental analysis. Fesenius J Anal Chem, 366, 769–779.
    10. Pleiss, J. (2000). In silico-Assays: Computergestuetzte Modellierung der Stereoselektivität von Lipasen. Transkript, 9, 38–40.
    11. Pleiss, J., Scheib, H., & Schmid, R. (2000). The his gap motif in microbial lipases: a determinant of stereoselectivity toward triacylglycerols and analogs. Biochimie, 82, 1043–1052.
    12. Hwang, B., Scheib, H., Pleiss, J., Kim, B., & Schmid, R. (2000). Computer-aided molecular modeling of the enantioselectivity of Pseudomonas cepacia lipase toward g- and d-lactones. J Mol Catal B Enzym, 10, 223–231.
    13. Enzelberger, M., Minning, S., & Schmid, R. (2000). Designing new metal affinity peptides by random mutagenesis of a natural metal-binding site. J Chromatogr A, 898, 83–94.
    14. Bachmann, T., Leca, B., Villatte, F., Marty, J., Fournier, D., & Schmid, R. (2000). Improved multianalyte detection of organophosphates and carbamates with disposable multielectrode biosensors using recombinant mutants of Drosophila acetylcholinesterase and artificial neural networks. Biosens Bioelectron, 15, 193–201.
    15. Zocher, F., Enzelberger, M., Bornscheuer, U., Hauer, B., Wohlleben, W., & Schmid, R. (2000). Epoxide hydrolase activity of Streptomyces strains. J Biotechnol, 77, 287–292.
    16. Schulz, T., Pleiss, J., & Schmid, R. (2000). Stereoselectivity of Pseudomonas cepacia lipase towards secondary alcohols: a quantitative model. Protein Sci, 9, 1053–1062.
    17. Schwaneberg, U., Fischer, P., & Schmid, R. (2000). Directed evolution of the fatty-acid hydroxylase P450 BM-3 into an indole-hydroxylating catalyst. Chemistry, 6, 1531–1536.
    18. Köhler, S., Bachmann, T., Schmitt, J., Belkin, S., & Schmid, R. (2000). Detection of 4-chlorobenzoate using immobilized recombinant Escherichia coli reporter strains. Sens Actuators B, 70, 139–144.
  24. 1999

    1. Scheib, H., Pleiss, J., Kovac, A., Paltauf, F., & Schmid, R. (1999). Stereoselectivity of Mucorales lipases toward triradylglycerols--a simple solution to a complex problem. Protein Sci, 8, 215–221.
    2. Cuong, N., Bachmann, T., & Schmid, R. (1999). Development of a dipstick immunoassay for quantitative determination of 2,4-dichlorophenoxyacetic acid in water, fruit and urine samples. Fresenius J Anal Chem, 364, 584–589.
    3. Bornscheuer, U., & Schmid, R. (1999). Lipase-catalyzed solid-phase synthesis of sugar fatty acid esters. Removal of by-products by azeotropic distillation. Enzyme Microb Technol, 25, 725–728.
    4. Zocher, F., Enzelberger, M., Bornscheuer, U., Hauer, B., & Schmid, R. (1999). A colorimetric assay suitable for screening epoxide hydrolase activity. Anal Chim Acta, 391, 345–351.
    5. Minning, S., Scheib, H., Traub, P., Schmitt, J., & Schmid, R. (1999). A toolbox of recombinant microbial lipases. In G. Kokotos (Ed.), Lipases and Lipids Structure, function and biotechnological applications Anwendungen (pp. 313–332). Crete University Press.
    6. Pleiss, J., & Schmid, R. (1999). Bioinformatics and the internet. Chemistry International, 21, 33–36.
    7. Shumyantseva, V., Bulko, T., Alexandrova, S., Sokolov, N., Bachmann, T., Schmid, R., & Archakov, A. (1999). N-terminal truncated cytochrome P450 2B4:  catalytic activities and reduction with alternative electron sources. Biochem Biophys Res Commun, 263, 678–680.
    8. Pleiss, J., Mionetto, N., & Schmid, R. (1999). Probing the acyl binding site of acetylcholinesterase by protein engineering. J Mol Catal B: Enzym, 6, 287–296.
    9. Schwaneberg, U., Schmidt-Dannert, C., Schmitt, J., & Schmid, R. (1999). A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Anal Biochem, 269, 359–366.
    10. Minning, S., Weiss, A., Bornscheuer, U., & Schmid, R. (1999). Determination of peracid and putative enzymatic peracid formation by an easy colorimetric assay. Anal Chim Acta, 378, 293–298.
    11. König, A., Bachmann, T., Metzger, J., & Schmid, R. (1999). Disposable sensor for measuring the biochemical oxygen demand for nitrification and inhibition of nitrification in wastewater. Applied Microbiology and Biotechnology, 51, 112–117.
    12. Bornscheuer, U., & Schmid, R. (1999). Lipase-catalyzed synthesis of vitamin c fatty acid esters. Biotechnol Lett, 21, 1051–1054.
    13. Khalameyzer, V., Fischer, I., Bornscheuer, U., & Altenbuchner, J. (1999). Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Appl Environ Microbiol, 65, 477–482.
    14. Soumanou, M., Bornscheuer, U., Schmid, U., & Schmid, R. (1999). Crucial role of support and water activity on the lipase-catalyzed synthesis of structured triglycerides. Biocatal Biotransform, 16, 443–459.
    15. Hauer, B., Schmid, R., Enzelberger, M., & Minning, S. (1999). Peptides for creation of fusion proteins and their purification by metal ion affinity chromatography. WO, 9960134.
    16. Schmid, U., Bornscheuer, U., Soumanou, M., McNeill, G., & Schmid, R. (1999). Highly selective synthesis of 1,3-oleoyl-2-palmitoylglycerol by lipase catalysis. Biotechnol Bioeng, 64, 678–684.
    17. Bachmann, T., & Schmid, R. (1999). A disposable multielectrode biosensor for the discrimination of organophosphate and carbamate insecticides in the submicromolar range using native and recombinant variants of acetylcholinesterase. Anal Chim Acta, 401, 95–103.
    18. McNiven, S., Yano, K., Ikebukuro, K., Bornscheuer, U., Schmid, R., & Karube, I. (1999). Highly sensitive trilayer piezoelectric odor sensor. Anal Chim Acta, 387, 39–45.
    19. Bornscheuer, U., & Schmid, R. (1999). Lipase-catalyzed solid-phase synthesis of sugar esters. Influence of immobilization on productivity and stability of the enzyme. J Mol Catal B Enzym, 6, 279–285.
    20. Quyen, D. T., Schmidt-Dannert, C., & Schmid, R. (1999). High-level formation of active Pseudomonas cepacia lipase after heterolgous expression of the encoding gene and its modified chaperone in Escherichia coli and rapid in vitro refolding. Appl Environ Microbiol, 65, 787–794.
    21. Schwaneberg, U., Sprauer, A., Schmidt-Dannert, C., & Schmid, R. (1999). P450 monooxygenase in biotechnology 1. Single-step, large-scale purification method for cytochrome P450 BM-3 by anion-exchange chromatography. J Chromatogr A, 848, 149–159.
  25. 1998

    1. Otto, R., Bornscheuer, U., Syldatk, C., & Schmid, R. (1998). Synthesis of aromatic n-alkyl-glucoside esters in a coupled beta-glucosidase and lipase reaction. Biotechnology Letters, 20, 437–440.
    2. Bornscheuer, U., & Schmid, R. (1998). Lipase-catalyzed solid-phase synthesis of sugar esters, IV: Selectivity of lipases towards primary and secondary hydroxyl groups in carbohydrates. Biocatal Biotransform, 16, 249–257.
    3. Soumanou, M., Bornscheuer, U., & Schmid, R. (1998). Two-step enzymatic reaction for the synthesis of pure structured triacylglycerides. J Am Oil Chem Soc, 75, 703–710.
    4. Soumanou, M., Bornscheuer, U., Schmid, U., & Schmid, R. (1998). Synthesis of structured triglycerides by lipase catalysis. Fett/Lipid, 100, 156–160.
    5. Bäumner, A., & Schmid, R. (1998). Development of a new immunosensor for pesticide detection: a disposable system with lipsome-enhancement and amperometric detection. Biosens Bioelectron, 13, 519–529.
    6. Schmidt-Dannert, C., Pleiss, J., & Schmid, R. (1998). A toolbox of recombinant lipases for industrial applications. Ann N Y Acad Sci, 864, 14–22.
    7. Lutz-Wahl, S., Fischer, P., Schmidt-Dannert, C., Wohlleben, W., & Schmid, R. (1998). Stereo- and regioselective hydroxylation of alpha-ionone by Streptomyces strains. Appl Environ Microbiol, 64, 3878–3881.
    8. Heim, J., Schmidt-Dannert, C., Atomi, H., & Schmid, R. (1998). Functional expression of a mammalian acetylcholinesterase in Pichia pastoris: comparison to acetylcholinesterase, expressed and reconstituted from Escherichia coli. Biochim Biophys Acta, 1396, 306–319.
    9. Wagegg, T., Enzelberger, M., Bornscheuer, U., & Schmid, R. (1998). The use of methoxy acetoxy esters significantly enhances reaction rates in the lipase-catalyzed preparation of enantiopure 1-(4-chloro phenyl) ethyl amines. J Biotechnol, 61, 75–78.
    10. Rua, M., Atomi, H., Schmidt-Dannert, C., & Schmid, R. (1998). High-level expression of the thermoalkalophilic lipase from Bacillus thermocatenulatus in Escherichia coli. Appl Microbiol Biotechnol, 49, 405–410.
    11. Schmid, R., & Verger, R. (1998). Lipases: interfacial enzymes with attractive applications. Angew Chem Int Ed, 37, 1608–1633.
    12. Beer, H., McCarthy, J., Bornscheuer, U., & Schmid, R. (1998). Cloning, expression, characterization and role of the leader sequence of a lipase from Rhizopus oryzae. Biochim Biophys Acta, 1399, 173–180.
    13. Bachmann, T., Bilitewski, U., & Schmid, R. (1998). A microbial sensor based on Pseudomonas putida for phenol, benzoic acid and their monochlorinated derivatives which can be used in water and n-hexane. Anal Lett, 31, 2361–2373.
    14. Scheib, H., Pleiss, J., Stadler, P., Kovac, A., Potthoff, A., Haalck, L., Spener, F., Paltauf, F., & Schmid, R. (1998). Rational design of Rhizopus oryzae lipase with modified stereoselectivity toward triradylglycerols. Protein Eng, 11, 675–682.
    15. Takahashi, S., Ueda, M., Atomi, H., Beer, H., Bornscheuer, U., Schmid, R., & Tanaka, A. (1998). Extracellular production of active Rhizopus oryzae lipase by Saccharomyces cerevisiae. J Ferment Bioeng, 86, 164–168.
    16. Beyersdorf-Radeck, B., Riedel, K., Karlson, U., Bachmann, T., & Schmid, R. (1998). Screening of xenobiotic compounds degrading microorganisms using biosensor techniques. Microbiol Res, 153, 239–245.
    17. Otto, R., Bornscheuer, U., Syldatk, C., & Schmid, R. (1998). Lipase-catalyzed solid phase synthesis of 6-O-monoesters from beta-D(+)-glucose and aromatic acids. Synthesis.
    18. Mosiello, L., Segre, L., Chiavarini, S., Spano, M., Cremisini, C., Kimmel, T., Bäumner, A., & Schmid, R. (1998). Dipstick immunoassay format for atrazine and terbuthylazine analysis in water samples. J Agric Food Chem, 46, 3847–3851.
    19. Yano, K., Karube, I., Bornscheuer, U., & Schmid, R. (1998). Development of an odorant sensor using polymer-coated quartz crystals modified with unusual lipids. Biosens Bioelectron, 13, 397–405.
    20. Hülser, D., Eckert, R., Irmer, U., Krisciukaitis, A., Mindermann, A., Pleiss, J., Rehkopf, B., Sharovskaya, J., & Traub, O. (1998). Intercellular communication via gap junction channels. Bioelectrochem Bioenerg, 45, 55–65.
    21. Pleiss, J., Fischer, M., & Schmid, R. (1998). Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids, 93, 67–80.
    22. Mindermann, A., Pleiss, J., & Hülser, D. (1998). Molecular Modeling of Gap Junction Pores. In R. Werner (Ed.), Gap Junctions. Proceedings of the 8th International Gap Junction Conference, Key Largo, Florida (pp. 67–71). IOS Press.
    23. Rubtsova, M., Wittmann, C., Egorov, A., & Schmid, R. (1998). Chemiluminescent immunoassay: application of a portable scanning luminometer for the determination of 2,4-dichlorophenoxyacetic acid in microtiter and membrane strip format. Food Agric Immunol, 9, 235–247.
    24. Minning, S., Schmidt-Dannert, C., & Schmid, R. (1998). Functional expression of Rhizopus oryzae lipase in Pichia pastoris: high-level production and some properties. J Biotechnol, 66, 147–156.
    25. Beimhorn, D., Flemming, H., Grummt, T., Hansen, P., Hock, B., Kanne, R., Kohler, H., Ludwig, W., & Obst, U. (1998). Bioeffects-related environmental analytics. Part 1. Limits of chemical and biological analytics. Labor-Fachzeitschrift, 42, 905–908.
    26. Drees, R., Pleiss, J., Schmid, R., & Roller, D. (1998). Integrating molecular modeling tools and virtual reality engines: an architecture for a highly immersive molecular modeling (HIMM) environment. Proceedings of CGI, 391–392.
    27. Brocca, S., Schmidt-Dannert, C., Lotti, M., Alberghina, L., & Schmid, R. (1998). Design, total synthesis, and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase. Protein Sci, 7, 1415–1422.
    28. Schmid, U., Bornscheuer, U., Soumanou, M., McNeill, G., & Schmid, R. (1998). Optimization of the reaction conditions in the lipase-catalyzed synthesis of structured triglycerides. J Am Oil Chem Soc, 75, 1527–1531.
    29. Soumanou, M., Schmid, U., Bornscheuer, U., & Schmid, R. (1998). Lipase-katalysierte Synthese von strukturierten Triglyceriden. Schriftenreihe, 10, 184–190.
    30. Rubtsova, M., Egorov, A., & Schmid, R. (1998). Simultaneous determination of several pesticides with chemiluminescent immunoassay on a multi-spot membrane strip. Food Agric Immunol, 10, 223–235.
    31. Bornscheuer, U., Enzelberger, M., & Altenbuchner, J. (1998). Mutator Strain Epicurian coli XL1-Red Generates Esterase Variants. Strategies Newsletter, 11, 16–17.
    32. Otto, R., Bornscheuer, U., Scheib, H., Pleiss, J., Syldatk, C., & Schmid, R. (1998). Lipase-catalyzed esterification of unusual substrates: synthesis of glucuronic acid and ascorbic acid. Biotechnol Lett, 20, 1091–1094.
    33. Kisselev, P., Wessel, R., Pisch, S., Bornscheuer, U., Schmid, R., & Schwarz, D. (1998). Branched phosphatidylcholines stimulate activity of cytochrome P450SCC (CYP11A1) in phospholipid vesicles by enhancing cholesterol binding, membrane incorporation and protein exchange. J Biol Chem, 273, 1380–1386.
    34. Enzelberger, M., Zocher, F., Bornscheuer, U., Schmidt-Dannert, C., Hauer, B., & Schmid, R. (1998). Singularisation of enzyme mutants by use of a cell sorter and the green fluorescent protein. Bioforum, 21, 192–194.
  26. 1997

    1. Pleiss, J., Mionetto, N., & Schmid, R. (1997). Protein engineering of rat brain acetylcholinesterase: a point mutation enhances sensitivityto pesticides. Protein Eng, 10, 66–66.
    2. Wittmann, C., & Schmid, R. (1997). Bioaffinity sensors for environmental monitoring. In E. Kress-Rogers (Ed.), Handbook of Biosensors and Electronic Noses: Medicine, Food and the Environment (pp. 333–347). CRC Press.
    3. Schrag, J., Cygler, M., Lang, D., Burgdorf, T., Hecht, H., Schmid, R., Schomburg, D., & Rydel, T. (1997). The open conformation of a Pseudomonas lipase. Structure, 5, 187–202.
    4. Kalisz, H., Hendle, J., & Schmid, R. (1997). Structural and biochemical properties of glycosylated and deglycosylated glucose oxidase from Penicillium amagasakiense. Appl Microbiol Biotechnol, 47, 502–507.
    5. Yano, K., Yoshitake, H., Bornscheuer, U., Schmid, R., Ikebukuro, K., Yokoyama, K., Masuda, Y., & Karube, I. (1997). Development of a chemical vapor sensor using piezoelectric quartz crystals with coated unusual lipids. Anal Chim Acta, 340, 41–48.
    6. Schwarz, D., Kisselev, P., Wessel, R., Pisch, S., Bornscheuer, U., & Schmid, R. (1997). Possible involvement of nonbilayer lipids in the stimulation of the activity of cytochrome P450SCC (CAP11A1) and its propensity to induce vesicle aggregation. Chem Phys Lipids, 85, 91–99.
    7. Mionetto, A., & Morel, N. (1997). Biochemical determination of insecticides via cholinesterases. 1. Acetylcholinesterase from rat brain: functional expression using a baculovirus system, and biochemical characterization. Biotechnol Tech, 11, 805–812.
    8. Schmidt-Dannert, C., Rua, M., & Schmid, R. (1997). Two novel lipases from the thermophile Bacillus thermocatenulatus: cloning, overexpression in E. coli, purification and properties. Methods Enzymol, 284, 194–220.
    9. Enzelberger, M., Bornscheuer, U., Gatfield, I., & Schmid, R. (1997). Lipase-catalysed resolution of gamma- and delta-lactones. J Biotechnol, 56, 129–133.
    10. Schwarz, D., Kisselev, P., Pfeil, W., Pisch, S., Bornscheuer, U., & Schmid, R. (1997). Evidence that nonbilayer phase propensity of the membrane is important for the side chain cleavage activity of cytochrome P450SCC. Biochemistry, 36, 14262–14270.
    11. Nishihara, H., Okamura, T., Schmid, R., Hauck, A., & Reuss, M. (1997). Biotechnological potential of P450 monooxygenases. High-level production of bovine cytochrome P450c17 monooxygenase during medium cell density culture of a recombinant yeast, Saccharomyces cerevisiae GRF 18 (YEp-Toku1). J Biotechnol, 56, 57–61.
    12. Schmidt-Dannert, C., Rua, M., Wahl, S., & Schmid, R. (1997). Bacillus thermocatenulatus lipase: a thermoalkalophilic lipase with interesting properties. Biochem Soc Trans, 25, 178–182.
    13. Peters, H., Schmidt-Dannert, C., & Schmid, R. (1997). The photoreaction center of Rhodobacter sphaeroides. Mater Sci Eng, C 4, 227–232.
    14. Soumanou, M., Bornscheuer, U., Menge, U., & Schmid, R. (1997). Synthesis of structured triglycerides from peanut oil with immobilized lipase. J Am Oil Chem Soc, 74, 427–433.
    15. Holzwarth, H.-C., Pleiss, J., & Schmid, R. (1997). Computer-aided modelling of stereoselective triglyceride hydrolysis catalyzed by Rhizopus oryzae lipase. J Mol Catal B Enzym, 3, 73–82.
    16. Catoni, E., Schmidt-Dannert, C., Brocca, S., & Schmid, R. (1997). Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: high-level production and some properties of functional expressed lipase B. Biotechnol Tech, 11, 689–695.
    17. Wittmann, C., Schmid, R., Löffler, S., & Zell, A. (1997). Application of a neural network for pattern recognition of pesticides in water samples by different immunochemical techniques. In E. M. Aga, D.S.; Thurman (Ed.), ACS Symposium Series No. 657, Immunochemical Technology for Environmental Applications (pp. 343–360). Oxford University Press.
    18. Weber, H., Zuegg, J., Faber, J., & Pleiss, J. (1997). Molecular reasons for lipase-sensitivity against acetaldehyde. J Mol Catal B: Enzym, 3, 131–138.
    19. Rua, M., Schmidt-Dannert, C., Wahl, S., Sprauer, A., & Schmid, R. (1997). Thermoalkalophilic lipase of Bacillus thermocatenulatus large-scale production, purification and properties: aggregation behaviour and its effect on activity. J Biotechnol, 56, 89–102.
    20. Pisch, S., Bornscheuer, U., Meyer, M., & Schmid, R. (1997). Properties of unusual phospholipids .4. Chemoenzymatic synthesis of phospholipids bearing acetylenic fatty acids. Tetrahedron, 53, 14627–14634.
    21. Fischer, A., Bornscheuer, U., & Schmid, R. (1997). Lipase-catalyzed solid phase synthesis of sugar fatty acid esters. Biocatalysis and Biotransformations, 14, 269–283.
    22. Haalck, L., Paltauf, F., Pleiss, J., Schmid, R., Spener, F., & Stadler, P. (1997). Stereoselectivity of lipase from Rhizopus oryzae toward triacylglycerols and anlogs: computer aided modelling and experimental validation. Methods Enzymol, 284, 353–376.
    23. Wittmann, C., Riedel, K., & Schmid, R. (1997). Microbial and enzyme sensors for environmental monitoring. In E. Kress-Rogers (Ed.), Handbook of Biosensors and Electronic Noses: Medicine, Food and the Environment (pp. 299–332). CRC Press.
  27. 1996

    1. Bornscheuer, U., & Schmid, R. (1996). Lipase-catalyzed solid-phase synthesis of sugar esters. Lipid/Fett, 98, 332–335.
    2. Schwarz, D., Kisselev, P., Wessel, R., Jüptner, O., & Schmid, R. (1996). Alpha-branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1). Modeling the structure of the fatty acyl chain region of cardiolipin. Journal of Biological Chemistry, 271, 12840–12846.
    3. Bäumner, A., Kummer, T., & Schmid, R. (1996). Liposome-based immunosensors. 1. Influence of hapten spacer length on liposome binding efficiency. Anal Lett, 29, 2601–2613.
    4. Schmidt-Dannert, C., Rua, M., Atomi, H., & Schmid, R. (1996). Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. molecular cloning, nucleotide sequence, purification and some properties. BBA-Lipid Lipid Met, 1301, 105–114.
    5. Bornscheuer, U., Gaziola, L., & Schmid, R. (1996). Application of vinyl esters for the lipase-catalyzed high-yield synthesis of monoacylglycerols. Ann NY Acad Sci, 799, 757–761.
    6. Heidt, M., Bornscheuer, U., & Schmid, R. (1996). Studies on the enantioselectivity in the lipase-catalyzed synthesis of  monoacylglycerols from isopropylidene glycerol. Biotechnol Tech, 10, 25–30.
    7. Gaziola, L., Bornscheuer, U., & Schmid, R. (1996). A rapid and effective separation of enantiomers of glycerol derivatives by gas chromatography and their lipase-catalyzed biotransformation. Enantiomer, 1, 49–54.
    8. Beer, H., Wohlfahrt, G., Schmid, R., & McCarthy, J. (1996). The folding and activity of the extracellular lipase of Rhizopus oryzae are modulated by a prosequence. Biochem J, 319, 351–359.
    9. Wittmann, C., Bilitewski, U., Giersch, T., Kettling, U., & Schmid, R. (1996). Development and evaluation of a dipstick immunoassay format for the determination of atrazine residues on-site. Analyst, 121, 863–869.
    10. Smidt, H., Fischer, A., Fischer, P., & Schmid, R. (1996). Preparation of optically pure chiral amines by lipase-catalyzed enantioselective hydrolysis of N-acyl-amines. Biotechnol Tech, 10, 335–338.
    11. Drees, R., Pleiss, J., & Schmid, R. (1996). Highly immersive molecular modeling (HIMM): an architecture for the integration of molecular modelling and virtual reality. In R. Hofestädt, M. Löffler, & D. Schomburg (Eds.), Computer science and biology : proceedings of the German Conference on Bioinformatics (GCB 96) (pp. 190–192). Universität Leipzig.
    12. Lang, D., Hofmann, B., Haalck, L., Hecht, H., Spener, F., Schmid, R., & Schomburg, D. (1996). Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution. J Mol Biol, 259, 704–717.
    13. Beer, H., Wohlfahrt, G., McCarthy, J., Schomburg, D., & Schmid, R. (1996). Analysis of the catalytic mechanism of a fungal lipase using computer-aided design and structural mutants. Protein Eng, 9, 507–517.
  28. 1995

    1. Schmid, R., Chung, B., Jones, A., Saono, S., Scriven, J., & Tsai, J. (1995). Biotechnology: a Multi-Volume Comprehensive Treatise. In H. Rehm, G. Reed, & D. Bauer (Eds.), Modern Biotechnology: Legal, Economic and Ethical Dimensions. (pp. 371–432). Wiley-VCH.
    2. Schmid, R. (1995). In Vorbereitung auf große Wachstumsmärkte: Biotechnologie und Gentechnik in Japan, Korea, China und Taiwan. Pharmazeutische Industrie, 57, 370–379.
    3. Schmid, R., Menge, U., Schomburg, D., & Spener, F. (1995). Towards novel biocatalysts via protein design: the case of lipases. FEMS Microbiol Rev, 16, 253–253.
    4. Westerhausen, M., Enzelberger, M., & Schwarz, W. (1995). Reaction of magnesium and calcium bisbis(trimethylsilyl)phosphanide with bisbis(trimethylsilyl)aminostannylene in a toluene solution. J Organomet Chem, 491, 83–90.
  29. 1994

    1. Pleiss, J. (1994). Molecular basis of specificity and stereoselectivity of microbial lipases toward triacylglycerols. In U. T. Bornscheuer (Ed.), Enzymes in Lipid Modification (pp. 85–99). Wiley-VCH.
    2. Rurup, J., Lauer, F., Drewes, A., Wray, V., & Schmid, R. (1994). Properties of unusual phospholipids, II: Synthesis, NMR studies and monolayer investigations of diacylglycerophosphocholines containing alpha-branched acyl chains. Chem Phys Lipids, 72, 175–183.
    3. Pleiss, J. (1994). Quantitative modelling of lipase enantioselectivity. In A. Svendsen (Ed.), Enzyme functionality: Design, engineering, and screening. Marcel Dekker.
    4. Rurup, J., Mannova, M., Brezesinki, G., & Schmid, R. (1994). Properties of unusual phospholipids: I. Synthesis, monolayer investigations and calorimetry of diacylglycerophosphocholines containing monoacetylenic acyl chains. Chemistry and Physics of Lipids, 70, 187–198.
  30. 1992

    1. Pleiss, J., & Jähnig, F. (1992). Conformational transition of an alpha-helix studied by molecular dynamics. Eur Biophys J, 21, 63–70.
  31. 1991

    1. Pleiss, J., & Jähnig, F. (1991). Collective vibrations of an alpha-helix. A molecular dynamics study. Biophys J, 59, 795–804.
  32. 1989

    1. Roditi, I., Schwarz, H., Pearson, T., Beecroft, R., Liu, M., Richardson, J., Bühring, H., Pleiss, J., Bülow, R., & et, al. (1989). Procyclin gene expression and loss of the variant surface glycoprotein during differentiation of Trypanosoma brucei. J Cell Biol, 108, 737–746.
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