Prof. Dr. Rebecca Buller

Projekte

• National Competence Center of Research Catalysis / Projektleiter:in / laufend
• Enzymatic Construction of DNA-Encoded Chemical Libraries / Projektleiter:in / abgeschlossen
• Biocatalytic halogenation for the sustainable development of agrochemicals / Projektleiter:in / abgeschlossen
• NCCR Catalysis / Teammitglied / abgeschlossen
• Strategien zur Reduktion von Mykotoxinen in Getreidenebenproduktströmen / Co-Projektleiter:in / abgeschlossen
• Microbial Epimerases: A Toolbox for the Synthesis of Novel Peptide-Based Drugs / Projektleiter:in / abgeschlossen
• Impulse - Digitalization in biofabrication: Design, recombinant production and testing of innovative Protein scaffolds as inks for 3D bioprinting / Stellv. Projektleiter:in / abgeschlossen
• Biocatalytic oxidation processes with alpha-ketoglutarate dependent enzymes for sustainable chemical synthesis / Projektleiter:in / abgeschlossen
• CAS - Biocatalysis / Stellv. Projektleiter:in / abgeschlossen
• PgB P-14 Engineered Halogenases / Projektleiter:in / abgeschlossen
• Biocatalytic Production - Engineering of terpene cyclases for the production of R-alpha-Ionone / Projektleiter:in / abgeschlossen
• Firmenich CTI 25929.2 / Projektleiter:in / abgeschlossen
• Innovationsraum Biokatalyse P-14 / Projektleiter:in / abgeschlossen

Publikationen

Beiträge in wissenschaftlicher Zeitschrift, peer-reviewed

• Özgen, F. F., Stockinger, P., Komarova, A. O., Luterbacher, J., & Buller, R. (2026). Biomass-derived diformylxylose as a renewable solvent for biocatalysis applications. ChemSusChem, 19(4), e202502273. https://doi.org/10.1002/cssc.202502273
• Schaub, D., Lessing, A., von Haugwitz, G., Meyer, F., Scheuermann, J., & Buller, R. (2026). Toward the chemoenzymatic synthesis of DNA-encoded libraries. ACS Central Science, 12(1), 28–39. https://doi.org/10.1021/acscentsci.5c01516
• Hecht, K., & Buller, R. (2025). Industrializing biocatalysis. Chimia, 79(7-8), 522–527. https://doi.org/10.2533/chimia.2025.522
• Graber, D., Stockinger, P., Meyer, F., Mishra, S., Horn, C., & Buller, R. (2025). Resolving data bias improves generalization in binding affinity prediction. Nature Machine Intelligence, 7(10), 1713–1725. https://doi.org/10.1038/s42256-025-01124-5
• Kumar, A., Taubitz, J., Meyer, F., Imstepf, N., Peng, J., Tassano, E., Moore, C., Lochmann, T., Šnajdrová, R., & Buller, R. (2025). Streamlining enzyme discovery and development through data analysis and computation. Chem Catalysis, 5(10), 101445. https://doi.org/10.1016/j.checat.2025.101445
• Vornholt, T., Stockinger, P., Mutný, M., Jeschek, M., Nestl, B. M., Oberdorfer, G., Osuna, S., Pleiss, J., Welner, D. H., Krause, A., Buller, R., & Ward, T. R. (2025). Of revolutions and roadblocks : the emerging role of machine learning in biocatalysis. ACS Central Science, 11(10), 1828–1838. https://doi.org/10.1021/acscentsci.5c00949
• Stockinger, P., Niederhauser, C., Farnaud, S., & Buller, R. (2025). Computational analysis reveals temperature-induced stabilization of FAST-PETase. Computational and Structural Biotechnology Journal, 27, 969–977. https://doi.org/10.1016/j.csbj.2025.03.006
• Buller, R., Damborsky, J., Hilvert, D., & Bornscheuer, U. T. (2024). Structure prediction and computational protein design for efficient biocatalysts and bioactive proteins. Angewandte Chemie: International Edition, 64(2), e202421686. https://doi.org/10.1002/anie.202421686
• Stockinger, P., & Buller, R. (2024). Nature’s toolbox for the hydrolysis of lactams and cyclic imides. ACS Catalysis, 14(21), 16055–16073. https://doi.org/10.1021/acscatal.4c04474
• Patsch, D., Schwander, T., Voss, M., Schaub, D., Hüppi, S., Eichenberger, M., Stockinger, P., Schelbert, L., Giger, S., Peccati, F., Jiménez-Osés, G., Mutný, M., Krause, A., Bornscheuer, U. T., Hilvert, D., & Buller, R. M. (2024). Enriching productive mutational paths accelerates enzyme evolution. Nature Chemical Biology, 20(12), 1662–1669. https://doi.org/10.1038/s41589-024-01712-3
• Bopp, C. E., Bernet, N. M., Meyer, F., Khan, R., Robinson, S. L., Kohler, H.-P. E., Buller, R., & Hofstetter, T. B. (2024). Elucidating the role of O2 uncoupling for the adaptation of bacterial biodegradation reactions catalyzed by Rieske oxygenases. ACS Environmental Au, 4(4), 204–218. https://doi.org/10.1021/acsenvironau.4c00016
• André, A., Hecht, K., Mischler, S., Stäheli, L., Kerhanaj, F., Buller, R., Kinner, M., Freimüller Leischtfeld, S., Chetschik, I., Miescher Schwenninger, S., & Müller, N. (2024). A new physical and biological strategy to reduce the content of zearalenone in infected wheat kernels : the effect of cold needle perforation, microorganisms, and purified enzyme. Food Research International, 186(114364). https://doi.org/10.1016/j.foodres.2024.114364
• Honda Malca, S., Stockinger, P., Duss, N., Milbredt, D., Iding, H., & Buller, R. (2024). Excelzyme : a Swiss university-industry collaboration for accelerated biocatalyst development. Chimia, 78(3), 108–117. https://doi.org/10.2533/chimia.2024.108
• Honda Malca, S., Duss, N., Meierhofer, J., Patsch, D., Niklaus, M., Reiter, S., Hanlon, S. P., Wetzl, D., Kuhn, B., Iding, H., & Buller, R. (2024). Effective engineering of a ketoreductase for the biocatalytic synthesis of an ipatasertib precursor. Communications Chemistry, 7(1), 46. https://doi.org/10.1038/s42004-024-01130-5
• Patsch, D., Eichenberger, M., Voss, M., Bornscheuer, U. T., & Buller, R. M. (2023). LibGENiE : a bioinformatic pipeline for the design of information-enriched enzyme libraries. Computational and Structural Biotechnology Journal, 21, 4488–4496. https://doi.org/10.1016/j.csbj.2023.09.013
• Eichenberger, M., Schwander, T., Hüppi, S., Kreuzer, J., Mittl, P. R. E., Peccati, F., Jiménez-Osés, G., Naesby, M., & Buller, R. M. (2023). The catalytic role of glutathione transferases in heterologous anthocyanin biosynthesis. Nature Catalysis, 6(10), 927–938. https://doi.org/10.1038/s41929-023-01018-y
• Buller, R., Lutz, S., Kazlauskas, R. J., Snajdrova, R., Moore, J. C., & Bornscheuer, U. T. (2023). From nature to industry : harnessing enzymes for biocatalysis. Science, 382(6673), eadh8615. https://doi.org/10.1126/science.adh8615
• Hegarty, E., Büchler, J., & Buller, R. M. (2023). Halogenases for the synthesis of small molecules. Current Opinion in Green and Sustainable Chemistry, 41(100784). https://doi.org/10.1016/j.cogsc.2023.100784
• Giger, S., & Buller, R. (2023). Advances in noncanonical amino acid incorporation for enzyme engineering applications. Chimia, 77(6), 395–402. https://doi.org/10.2533/chimia.2023.395
• Patsch, D., & Buller, R. (2023). Improving enzyme fitness with machine learning. Chimia, 77(3), 116–121. https://doi.org/10.2533/chimia.2023.116
• Voss, M., Hüppi, S., Schaub, D., Hayashi, T., Ligibel, M., Sager, E., Schroer, K., Snajdrova, R., & Buller, R. (2022). Enzyme engineering enables inversion of substrate stereopreference of the halogenase WelO5*. ChemCatChem, 14(24), e202201115. https://doi.org/10.1002/cctc.202201115
• Papadopoulou, A., Peters, C., Borchert, S., Steiner, K., & Buller, R. (2022). Development of an ene reductase-based biocatalytic process for the production of flavor compounds. Organic Process Research & Development, 26(7), 2102–2110. https://doi.org/10.1021/acs.oprd.2c00096
• Büchler, J., Hegarty, E., Schroer, K., Snajdrova, R., Turner, N. J., Loiseleur, O., Buller, R., & Le Chapelain, C. (2022). A collaborative journey towards the late‐stage functionalization of added‐value chemicals using engineered halogenases. Helvetica Chimica Acta, 106(1), e202200128. https://doi.org/10.1002/hlca.202200128
• Papadopoulou, A., Meyer, F., & Buller, R. M. (2022). Engineering Fe(II)/α-ketoglutarate-dependent halogenases and desaturases. Biochemistry, 62(2), 229–240. https://doi.org/10.1021/acs.biochem.2c00115
• Büchler, J., Honda Malca, S., Patsch, D., Voss, M., Turner, N. J., Bornscheuer, U. T., Allemann, O., Le Chapelain, C., Lumbroso, A., Loiseleur, O., & Buller, R. (2022). Algorithm-aided engineering of aliphatic halogenase WelO5* for the asymmetric late-stage functionalization of soraphens. Nature Communications, 13(371). https://doi.org/10.1038/s41467-022-27999-1
• Eichenberger, M., Hüppi, S., Patsch, D., Aeberli, N., Berweger, R., Dossenbach, S., Eichhorn, E., Flachsmann, F., Hortencio, L., Voirol, F., Vollenweider, S., Bornscheuer, U. T., & Buller, R. (2021). Asymmetric cation-olefin monocyclization by engineered squalene-hopene cyclases. Angewandte Chemie: International Edition, 60(50), 26080–26086. https://doi.org/10.1002/anie.202108037
• Reiter, M., Hevey, R., Buller, R., & Shybeka, I. (2021). Swiss women in chemistry – two years later ... Chimia, 75(12), 1088–1090. https://doi.org/10.2533/chimia.2021.1088
• Papadopoulou, A., Meierhofer, J., Meyer, F., Hayashi, T., Schneider, S., Sager, E., & Buller, R. (2021). Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate. ChemCatChem, 13(18), 3914–3919. https://doi.org/10.1002/cctc.202100591
• Meyer, F., Frey, R., Ligibel, M., Sager, E., Schroer, K., Snajdrova, R., & Buller, R. (2021). Modulating chemoselectivity in a Fe(II)/α-ketoglutarate-dependent dioxygenase for the oxidative modification of a non-proteinogenic amino acid. ACS Catalysis, 2021(11). https://doi.org/10.1021/acscatal.1c00678
• Hecht, K., Meyer, H.-P., Wohlgemuth, R., & Buller, R. (2020). Biocatalysis in the Swiss manufacturing environment. Catalysts, 10(12), 1420. https://doi.org/10.3390/catal10121420
• Voss, M., Küng, R., Hayashi, T., Jonczyk, M., Niklaus, M., Iding, H., Wetzl, D., & Buller, R. (2020). Multi‐faceted set‐up of a diverse ketoreductase library enables the synthesis of pharmaceutically‐relevant secondary alcohols. ChemCatChem, 13(6), 1538–1545. https://doi.org/10.1002/cctc.202001871
• Aregger, D., Peters, C., & Buller, R. (2020). Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa. Catalysts, 10(2). https://doi.org/10.3390/catal10020254
• Voss, M., Honda Malca, S., & Buller, R. (2020). Exploring the biocatalytic potential of Fe/α‐ketoglutarate dependent halogenases. Chemistry - A European Journal. https://doi.org/10.1002/chem.201905752
• Peters, C., & Buller, R. (2019). Linear enzyme cascade for the production of (–)-iso-isopulegol. Zeitschrift Für Naturforschung C, 74(3-4). https://doi.org/10.1515/znc-2018-0146
• Peters, C., & Buller, R. (2019). Industrial application of 2-oxoglutarate-dependent oxygenases. Catalysts, 9(3), 221–240. https://doi.org/10.3390/catal9030221
• Frey, R., Hayashi, T., & Buller, R. (2019). Directed evolution of carbon–hydrogen bond activating enzymes. Current Opinion in Biotechnology, 60, 29–38. https://doi.org/10.1016/j.copbio.2018.12.004
• Büchler, J., Papadopoulou, A., & Buller, R. (2019). Recent advances in Flavin-dependent halogenase biocatalysis : sourcing, engineering, and application. Catalysts, 9(12), 1030. https://doi.org/10.3390/catal9121030
• Hayashi, T., Ligibel, M., Sager, E., Voss, M., Hunziker, J., Schroer, K., Snajdrova, R., & Buller, R. (2019). Evolved aliphatic halogenases enable regiocomplementary C‐H functionalization of an added‐value chemical. Angewandte Chemie: International Edition, 58(51), 18535–18539. https://doi.org/10.1002/anie.201907245
• Hayashi, T., Ligibel, M., Sager, E., Voss, M., Hunziker, J., Schroer, K., Snajdrova, R., & Buller, R. (2019). Evolvierte aliphatische Halogenasen ermöglichen die regiokomplementäre C‐H‐Funktionalisierung einer hochwertigen Chemikalie. Angewandte Chemie, 131(51), 18706–18711. https://doi.org/10.1002/ange.201907245
• Papadopoulou, A., Hecht, K., & Buller, R. (2019). Enzymatic PET degradation. Chimia, 73(9), 743–749. https://doi.org/10.2533/chimia.2019.743
• Peters, C., Frasson, D., Sievers, M., & Buller, R. (2019). Novel Old Yellow Enzyme subclasses. ChemBioChem. https://doi.org/10.1002/cbic.201800770
• Blomberg, R., Kries, H., Pinkas, D. M., Mittl, P. R. E., Grütter, M. G., Privett, H. K., Mayo, S. L., & Hilvert, D. (2013). Precision is essential for efficient catalysis in an evolved Kemp eliminase. Nature, 503(7476), 418–421. https://doi.org/10.1038/nature12623
• Kries, H., Blomberg, R., & Hilvert, D. (2013). De novo enzymes by computational design. Current Opinion in Chemical Biology, 17(2), 221–228. https://doi.org/10.1016/j.cbpa.2013.02.012
• Privett, H. K., Kiss, G., Lee, T. M., Blomberg, R., Chica, R. A., Thomas, L. M., Hilvert, D., Houk, K. N., & Mayo, S. L. (2012). Iterative approach to computational enzyme design. Proceedings of the National Academy of Sciences of the United States of America, 109(10), 3790–3795. https://doi.org/10.1073/pnas.1118082108
• Richter, F., Blomberg, R., Khare, S. D., Kiss, G., Kuzin, A. P., Smith, A. J. T., Gallaher, J., Pianowski, Z., Helgeson, R. C., Grjasnow, A., Xiao, R., Seetharaman, J., Su, M., Vorobiev, S., Lew, S., Forouhar, F., Kornhaber, G. J., Hunt, J. F., Montelione, G. T., et al. (2012). Computational design of catalytic dyads and oxyanion holes for ester hydrolysis. Journal of the American Chemical Society, 134(39), 16197–16206. https://doi.org/10.1021/ja3037367
• Chapleau, R. R., Blomberg, R., Ford, P. C., & Sagermann, M. (2008). Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake. Protein Science, 17(4), 614–622. https://doi.org/10.1110/ps.073358908

Buchbeiträge, peer-reviewed

• Hecht, K., & Buller, R. (2019). Ene-reductases in pharmaceutical chemistry. In P. Grunwald (Ed.), Pharmaceutical biocatalysis : chemoenzymatic synthesis of active pharmaceutical ingredients. Jenny Stanford.
• Buller, R., Hecht, K., Mirata, M. A., & Meyer, H.-P. (2017). An appreciation of biocatalysis in the Swiss manufacturing environment. In Biocatalysis : an industrial perspective (pp. 1–43). Royal Society of Chemistry. https://doi.org/10.1039/9781782629993-00001

Weitere Publikationen

• Graber, D., Stockinger, P., Meyer, F., Mishra, S., Horn, C., & Buller, R. (2024). GEMS : a generalizable GNN framework for protein-ligand binding affinity prediction through robust data filtering and language model integration. bioRxiv. https://doi.org/10.1101/2024.12.09.627482
• André, A., Hecht, K., Mischler, S., Buller, R., Chetschik, I., Miescher Schwenninger, S., & Müller, N. (2024, November 4). A new physical and biological strategy to reduce the content of zearalenone in infected wheat kernels : the effect of cold needle perforation, microorganisms, and purified enzyme. 11th Symposium on Recent Advances in Food Analysis (RAFA), Prague, Czech Republic, 5-8 November 2024.
• Buller, R., Coperét, C., Emsley, L., Gademann, K., Hari, Y., & Leo, M. (2021). Chemistry roadmap for research infrastructures 2025-2028 by the Swiss chemistry community. Swiss Academy of Sciences. https://doi.org/10.5281/zenodo.4572642
• Buller, R. (2021). Biocatalysis and biosynthesis. In Technology Outlook 2021 (p. 71). Swiss Academy of Engineering Sciences SATW. https://www.satw.ch/de/publikationen/technology-outlook-2021

Mündliche Konferenzbeiträge und Abstracts

• André, A., Hecht, K., Mischler, S., Freimüller Leischtfeld, S., Kinner, M., Stäheli, L., Kerhanaj, F., Buller, R., Miescher Schwenninger, S., Chetschik, I., & Müller, N. (2023, October 6). Eine biologische Strategie zur Reduzierung des Zearalenongehalts in infizierten Weizenkörnern. 9. D-A-CH-Tagung für angewandte Getreidewissenschaften, Detmold, Deutschland, 5.-6. Oktober 2023.
• André, A., Freimüller Leischtfeld, S., Mischler, S., Hecht, K., Stäheli, L., Rüegg, R., Kinner, M., Buller, R., Chetschik, I., Miescher Schwenninger, S., & Müller, N. (2022, July 7). Mycotoxins reduction strategies to reintroduce grain side product streams into the food value chain. 20th ICC Conference, Vienna, Austria, 5-7 July 2022.

Forschungsdaten

Özgen, Fatma Feyza; Stockinger, Peter; Komarova, Anastasia; Luterbacher, Jeremy; Buller, Rebecca, 2025. Dataset for biomass-derived diformylxylose as a renewable solvent for biocatalysis applications. Zenodo. Verfügbar unter: https://doi.org/10.5281/zenodo.17286566

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