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Fraaije, Prof. Marco

Marco Fraaije
Marco Fraaije

Prof. Marco W. Fraaije studied Molecular Science at Wageningen University & Research, where he also gained his PhD. He was then a postdoctoral researcher at the Department of Genetics and Microbiology at the University of Pavia (Italy) and has worked at the University of Groningen since 1999. When he was an assistant professor, he led several studies centred around discovering new biocatalysts (enzymes) and researching their function.

At present, he is Professor of Molecular Enzymology. In 2016, he was awarded a Vici research grant and in 2018, he received the BIOCAT Science Award for his academic contribution to the biotechnology research field. Fraaije has published hundreds of articles, with a main focus on biocatalysis and enzyme engineering. His research revolves around discovering and designing new enzymes, focusing particularly on flavine adenine dinucleotide enzymes: those that use vitamin B2 to function.

In addition to the academic applications of his research, Fraaije is also building a bridge between the worlds of academia and industry. For example, he is the co-founder and current advisor of start-up company Gecco Biotech. Additionally, he has coordinated several EU-funded initiatives, among which the ROBOX project. This project is mainly aimed at designing robust enzymes that can be used in oxidation processes. These enzymes can replace chemical reactions that are currently being used in production processes. The aim is to reduce the need to use precious metals and toxic substances. Furthermore, his research group is working on computer-based engineering methods to adjust enzymes quickly for biotechnological applications.

2024

Guo, Y., Ashley, B., Marić, I., Saifuddin, M., Dunleavy, T., Onet, A., & Fraaije, M. W. (2024). Biocatalytic Oxidative Amination of para-Substituted Phenols. ChemCatChem, Article e202400277. Advance online publication. https://doi.org/10.1002/cctc.202400277
Russo, S., Rozeboom, H. J., Wijma, H. J., Poelarends, G. J., & Fraaije, M. W. (2024). Biochemical, kinetic, and structural characterization of a Bacillus tequilensis nitroreductase. The FEBS Journal, Article 17210. Advance online publication. https://doi.org/10.1111/febs.17210
Santema, L. L., Rotilio, L., Xiang, R., Tjallinks, G., Guallar, V., Mattevi, A., & Fraaije, M. W. (2024). Discovery and biochemical characterization of thermostable glycerol oxidases. Applied Microbiology and Biotechnology, 108(1), 1-14. Article 61. https://doi.org/10.1007/s00253-023-12883-9
Lee, M., & Fraaije, M. W. (2024). Equipping Saccharomyces cerevisiae with an Additional Redox Cofactor Allows F 420-Dependent Bioconversions in Yeast. ACS Synthetic Biology, 13(3), 921–929. https://doi.org/10.1021/acssynbio.3c00718
Yang, G., Pećanac, O., Wijma, H. J., Rozeboom, H. J., de Gonzalo, G., Fraaije, M. W., & Mascotti, M. L. (2024). Evolution of the catalytic mechanism at the dawn of the Baeyer-Villiger monooxygenases. Cell reports, 43(5), Article 114130. https://doi.org/10.1016/j.celrep.2024.114130
Boverio, A., Jamil, N., Mannucci, B., Mascotti, M. L., Fraaije, M. W., & Mattevi, A. (2024). Structure, mechanism, and evolution of the last step in vitamin C biosynthesis. Nature Communications, 15(1), Article 4158. https://doi.org/10.1038/s41467-024-48410-1
Russo, S., Prats Luján, A., Fraaije, M., & Poelarends, G. J. (2024). Synthesis of Pharmaceutically Relevant Arylamines Enabled by a Nitroreductase from Bacillus tequilensis. ChemBioChem, 25(10), Article e202300846. https://doi.org/10.1002/cbic.202300846
Fraaije, M. W., & Tong, Y. (2024). Variant flavoproteins comprising covalently tethered flavin cofactor, and means and methods related thereto. (Patent No. WO2024136655).

2023

Santema, L. L., Basile, L., Binda, C., & Fraaije, M. W. (2024). Discovery and structural characterization of a thermostable bacterial monoamine oxidase. The FEBS Journal, 291(5), 849-864. https://doi.org/10.1111/febs.16973
Rotilio, L., Boverio, A., Nguyen, Q.-T., Mannucci, B., Fraaije, M., & Mattevi, A. (2023). A biosynthetic aspartate N-hydroxylase performs successive oxidations by holding intermediates at a site away from the catalytic center. The Journal of Biological Chemistry, 299(7), Article 104904. https://doi.org/10.1016/j.jbc.2023.104904
Arentshorst, M., Kooloth Valappil, P., Mózsik, L., Regensburg-Tuïnk, T. J. G., Seekles, S., Tjallinks, G., Fraaije, M., Visser, J., & Ram, A. F. J. (2023). A CRISPR/Cas9-based multicopy integration system for protein production in Aspergillus niger. The FEBS Journal, 5127-5140. Article 16891. https://doi.org/10.1111/febs.16891
Marić, I., Guo, Y., Fürst, M. J. L. J., Van Aelst, K., Van den Bosch, S., De Simone, M., Martins, L. O., Sels, B. F., & Fraaije, M. W. (2023). A One-Pot, Whole-Cell Biocatalysis Approach for Vanillin Production using Lignin Oil. Advanced Synthesis and Catalysis, 365(22), 3987-3995. https://doi.org/10.1002/adsc.202300868
Boverio, A., van Beek, H. L., Savino, S., Ranoux, A., Huijgen, W. J. J., Raaijmakers, H. W. C., Fraaije, M. W., & Lončar, N. (2023). Biochemical and Structural Characterization of a Uronic Acid Oxidase from Citrus sinensis. ChemCatChem, 15(21), Article e202300847. https://doi.org/10.1002/cctc.202300847
Tong, Y., Rozeboom, H. J., Loonstra, M. R., Wijma, H. J., & Fraaije, M. W. (2023). Characterization of two bacterial multi-flavinylated proteins harboring multiple covalent flavin cofactors. BBA Advances, 4, Article 100097. https://doi.org/10.1016/j.bbadva.2023.100097
Tjallinks, G., Boverio, A., Jager, A. W., Kaya, S. G., Mattevi, A., & Fraaije, M. W. (2023). Efficient Oxidation of 5-Hydroxymethylfurfural Using a Flavoprotein Oxidase from the Honeybee Apis mellifera. ChemBioChem, 24(24), Article e202300588. https://doi.org/10.1002/cbic.202300588
Bailleul, G., Yang, G., Nicoll, C. R., Mattevi, A., Fraaije, M. W., & Mascotti, M. L. (2023). Evolution of enzyme functionality in the flavin-containing monooxygenases. Nature Communications, 14(1), Article 1042. https://doi.org/10.1038/s41467-023-36756-x
Tong, Y., Kaya, S. G., Russo, S., Rozeboom, H. J., Wijma, H. J., & Fraaije, M. W. (2023). Fixing Flavins: Hijacking a Flavin Transferase for Equipping Flavoproteins with a Covalent Flavin Cofactor. Journal of the American Chemical Society, 145(49), 27140–27148. https://doi.org/10.1021/jacs.3c12009
Yang, G., Wijma, H. J., Rozeboom, H. J., Mascotti, M. L., & Fraaije, M. W. (2023). Identification and characterization of archaeal and bacterial F420-dependent thioredoxin reductases. The FEBS Journal, 290(19), 4777-4791. https://doi.org/10.1111/febs.16896
Nicoll, C. R., Massari, M., Fraaije, M. W., Mascotti, M. L., & Mattevi, A. (2023). Impact of ancestral sequence reconstruction on mechanistic and structural enzymology. Current Opinion in Structural Biology, 82, Article 102669. https://doi.org/10.1016/j.sbi.2023.102669
Guo, Y., Alvigini, L., Saifuddin, M., Ashley, B., Trajkovic, M., Alonso-Cotchico, L., Mattevi, A., & Fraaije, M. W. (2023). One-pot biocatalytic synthesis of rac-syringaresinol from a lignin-derived phenol. ACS Catalysis, 13(22), 14639-14649. https://doi.org/10.1021/acscatal.3c04399
Tjallinks, G., Boverio, A., Maric, I., Rozeboom, H., Arentshorst, M., Visser, J., Ram, A. F. J., Mattevi, A., & Fraaije, M. W. (2023). Structure elucidation and characterization of patulin synthase, insights into the formation of a fungal mycotoxin. The FEBS Journal, 290(21), 5114-5126. Article 16804. https://doi.org/10.1111/febs.16804
Eggerichs, D., Weindorf, N., Mascotti, M. L., Welzel, N., Fraaije, M. W., & Tischler, D. (2023). Vanillyl alcohol oxidase from Diplodia corticola: Residues Ala420 and Glu466 allow for efficient catalysis of syringyl derivatives. The Journal of Biological Chemistry, 299(7), Article 104898. https://doi.org/10.1016/j.jbc.2023.104898

2022

de Gonzalo, G., Loncar, N., & Fraaije, M. (2024). Sulphoxidation reactions catalysed by the Baeyer-Villiger monooxygenase OTEMO from Pseudomonas putida ATCC 17453. Biocatalysis and Biotransformation, 42(1), 77-84. Article 2113519. https://doi.org/10.1080/10242422.2022.2113519
Boverio, A., Widodo, W. S., Santema, L. L., Rozeboom, H. J., Xiang, R., Guallar, V., Mattevi, A., & Fraaije, M. W. (2023). Structural Elucidation and Engineering of a Bacterial Carbohydrate Oxidase. Biochemistry, 62(2), 429-436. https://doi.org/10.1021/acs.biochem.2c00307
Partipilo, M., Yang, G., Mascotti, L., Slotboom, D., & Fraaije, M. (2022). A conserved sequence motif in the E. coli soluble FAD-containing pyridine nucleotide transhydrogenase is important for reaction efficiency. The Journal of Biological Chemistry, 298(9), Article 102304. https://doi.org/10.1016/j.jbc.2022.102304
Tong, Y., Loonstra, M. R., & Fraaije, M. (2022). Broadening the scope of the Flavin-tag method by improving flavin incorporation and incorporating flavin analogs. ChemBioChem, 23(11), Article e202200144. https://doi.org/10.1002/cbic.202200144
Venturi, S., Trajkovic, M., Colombo, D., Brenna, E., Fraaije, M. W., Gatti, F. G., Macchi, P., & Zamboni, E. (2022). Chemoenzymatic Synthesis of the Most Pleasant Stereoisomer of Jessemal. The Journal of Organic Chemistry, 87(9), 6499-6503. https://doi.org/10.1021/acs.joc.2c00427
de Gonzalo, G., Lončar, N., & Fraaije, M. (2022). Kinetic resolution of racemic benzofused alcohols catalysed by HMFO variants in presence of natural deep eutectic solvents. Biocatalysis and Biotransformation, 41(2), 145-152. https://doi.org/10.1080/10242422.2022.2038582
Guo, Y., Alvigini, L., Trajkovic, M., Alonso-Cotchico, L., Monza, E., Savino, S., Marić, I., Mattevi, A., & Fraaije, M. W. (2022). Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound. Nature Communications, 13(1), Article 7195. https://doi.org/10.1038/s41467-022-34912-3

2021

Gran-Scheuch, A., Parra, L., & Fraaije, M. W. (2023). Systematic Assessment of Uncoupling in Flavoprotein Oxidases and Monooxygenases. ACS Sustainable Chemistry and Engineering, 4948–4959. https://doi.org/10.1021/acssuschemeng.1c02012
Rembeza, E., Boverio, A., Fraaije, M. W., & Engqvist, M. (2022). Discovery of two novel oxidases using a high-throughput activity screen. ChemBioChem, 23(2), Article e202100510. https://doi.org/10.1002/cbic.202100510
Lee, M., Drenth, J., Trajkovic, M., de Jong, R. M., & Fraaije, M. W. (2022). Introducing an Artificial Deazaflavin Cofactor in Escherichia coli and Saccharomyces cerevisiae. ACS Synthetic Biology, 11(2), 938-952. https://doi.org/10.1021/acssynbio.1c00552
Drenth, J., Yang, G., Paul, C. E., & Fraaije, M. W. (2021). A Tailor-Made Deazaflavin-Mediated Recycling System for Artificial Nicotinamide Cofactor Biomimetics. ACS Catalysis, 11, 11561-11569. https://doi.org/10.1021/acscatal.1c03033
Laura, A., Gran-Scheuch, A., Guo, Y., Trajkovic, M., Saifuddin, M., Fraaije, M. W., & Mattevi, A. (2021). Discovery, Biocatalytic Exploration and Structural Analysis of a 4-Ethylphenol Oxidase from Gulosibacter chungangensis. ChemBioChem, 22(22), 3225-3233. Article cbic.202100457. https://doi.org/10.1002/cbic.202100457
Tjallinks, G., Martin, C., & Fraaije, M. W. (2021). Enantioselective oxidation of secondary alcohols by the flavoprotein alcohol oxidase from Phanerochaete chrysosporium. Archives of Biochemistry and Biophysics, 704, Article 108888. https://doi.org/10.1016/j.abb.2021.108888
Cibulka, R., & Fraaije, M. W. (2021). Flavin-Based Catalysis - Preface. In R. Cibulka, & M. Fraaije (Eds.), Flavin-Based Catalysis: Principles and Applications (pp. xi-xii). Wiley.
Tong, Y., Lee, M., Drenth, J., & Fraaije, M. W. (2021). Flavin-Tag: A Facile Method for Site-Specific Labeling of Proteins with a Flavin Fluorophore. BIOCONJUGATE CHEMISTRY, 32(8), 1559-1563. https://doi.org/10.1021/acs.bioconjchem.1c00306
Savino, S., Daniël‐Moráh Meijer, J., Rozeboom, H. J., van Beek, H. L., & Fraaije, M. W. (2021). Kinetic and structural properties of a robust bacterial L-amino acid oxidase. Catalysts, 11(11), Article 1309. https://doi.org/10.3390/catal11111309
Fraaije, M. W., Trajkovic, M., & Martin, C. (2021). Means and methods for selective double diol oxidation. (Patent No. WO2021071356).
Cibulka, R., & Fraaije, M. W. (2021). Modes of Flavin-Based Catalysis. In R. Cibulka, & M. W. Fraaije (Eds.), Flavin-Based Catalysis: Principles and Applications (pp. 97-124). Wiley. https://doi.org/10.1002/9783527830138.ch4
Purwani, N. N., Martin, C., Savino, S., & Fraaije, M. W. (2021). Modular assembly of phosphite dehydrogenase and phenylacetone monooxygenase for tuning cofactor regeneration. Biomolecules, 11(6), Article 905. https://doi.org/10.3390/biom11060905
Drenth, J., & Fraaije, M. W. (2021). Natural Flavins: Occurrence, Role, and Noncanonical Chemistry. In R. Cibulka, & M. W. F. (Eds.), Flavin-Based Catalysis: Principles and Applications (pp. 29-65). Wiley. https://doi.org/10.1002/9783527830138.ch2
Mascotti, M. L., Juri Ayub, M., & Fraaije, M. W. (2021). On the diversity of F420 -dependent oxidoreductases: A sequence- and structure-based classification. Proteins, 89(11), 1497-1507. Article 26170. https://doi.org/10.1002/prot.26170
Gran-Scheuch, A., Aalbers, F., Woudstra, Y., Parra, L., & Fraaije, M. W. (2021). Optimizing the linker length for fusing an alcohol dehydrogenase with a cyclohexanone monooxygenase. In M. Merkx (Ed.), Linkers in Biomacromolecules (Vol. 647, pp. 107-143). (Methods in Enzymology). Elsevier. https://doi.org/10.1016/bs.mie.2020.09.008
Lončar, N., Konukoglu, F., Fraaije, M., Eryilmaz, J., & Tuncer, E. (2021). Process for dyeing textiles. (Patent No. WO2021013371).
Zuccarello, L., Barbosa, C., Galdino, E., Lončar, N., Silveira, C. M., Fraaije, M. W., & Todorovic, S. (2021). Serr spectroelectrochemistry as a guide for rational design of dyp-based bioelectronics devices. International Journal of Molecular Sciences, 22(15), Article 7998. https://doi.org/10.3390/ijms22157998
Kardashliev, T., Weingartner, A., Romero, E., Schwaneberg, U., Fraaije, M., Panke, S., & Held, M. (2021). Whole-cell screening of oxidative enzymes using genetically encoded sensors. Chemical Science, 12(44), 14766-14772. Article d1sc02578c. https://doi.org/10.1039/d1sc02578c

2020

Bailleul, G., Nicoll, C. R., Mascotti, M. L., Mattevi, A., & Fraaije, M. W. (2021). Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties. The Journal of Biological Chemistry, 296, Article 100221. https://doi.org/10.1074/jbc.RA120.016297
Martin, C., Tjallinks, G., Trajkovic, M., & Fraaije, M. (2021). Facile Stereoselective Reduction of Prochiral Ketones by using an F 420-dependent alcohol dehydrogenase. ChemBioChem, 22(1), 156-159. Article cbic.202000651. https://doi.org/10.1002/cbic.202000651
Zitare, U. A., Habib, M. H., Rozeboom, H., Mascotti, M. L., Todorovic, S., & Fraaije, M. W. (2021). Mutational and structural analysis of an ancestral fungal dye decolorizing peroxidase. The FEBS Journal, 288(11), 3602-3618. Article febs.15687. https://doi.org/10.1111/febs.15687
Savino, S., Jensen, S., Terwisscha van Scheltinga, A., & Fraaije, M. W. (2020). Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines. FEBS Letters, 594(17), 2819-2828. https://doi.org/10.1002/1873-3468.13854
Aalbers, F. S., Fürst, M. J., Rovida, S., Trajkovic, M., Gómez Castellanos, J. R., Bartsch, S., Vogel, A., Mattevi, A., & Fraaije, M. W. (2020). Approaching boiling point stability of an alcohol dehydrogenase through computationally-guided enzyme engineering. eLife, 9, Article e54639. https://doi.org/10.7554/eLife.54639
Ueoka, R., Meoded, R. A., Gran-Scheuch, A., Bhushan, A., Fraaije, M. W., & Piel, J. (2020). Corrigendum to: Genome Mining of Oxidation Modules in trans -Acyltransferase Polyketide Synthases Reveals a Culturable Source for Lobatamides (Angewandte Chemie International Edition, (2020), 59, 20, (7761-7765), 10.1002/anie.201916005). Angewandte Chemie-International Edition, 59(29), 11698-11698. https://doi.org/10.1002/anie.202007393
Ueoka, R., Meoded, R., Gran-Scheuch, A., Bhushan, A., Fraaije, M., & Piel, J. (2020). Genome mining of oxidation modules in trans-acyltransferase polyketide synthases reveals a culturable source for lobatamides. Angewandte Chemie (International ed. in English), 59(20), 7761-7765. https://doi.org/10.1002/anie.201916005
Román, R., Lončar, N., Casablancas, A., Fraaije, M. W., & Gonzalez, G. (2020). High-level production of industrially relevant oxidases by a two-stage fed-batch approach: Overcoming catabolite repression in arabinose-inducible Escherichia coli systems. Applied Microbiology and Biotechnology, 104(12), 5337-5345. https://doi.org/10.1007/s00253-020-10622-y
Romero, E., Savino, S., Fraaije, M. W., & Loncar, N. (2020). Mechanistic and Crystallographic Studies of Azoreductase AzoA from Bacillus wakoensis A01. ACS chemical biology, 15(2), 504-512. Article acschembio.9b00970. https://doi.org/10.1021/acschembio.9b00970
Venturi, S., Brenna, E., Colombo, D., Fraaije, M. W., Gatti, F. G., Macchi, P., Monti, D., Trajkovic, M., & Zamboni, E. (2020). Multienzymatic Stereoselective Reduction of Tetrasubstituted Cyclic Enones to Halohydrins with Three Contiguous Stereogenic Centers. ACS Catalysis, 10(21), 13050-13057. https://doi.org/10.1021/acscatal.0c04097
de Gonzalo, G., Martin, C., & Fraaije, M. W. (2020). Positive Impact of Natural Deep Eutectic Solvents on the Biocatalytic Performance of 5-Hydroxymethyl-Furfural Oxidase. Catalysts, 10(4), Article 447. https://doi.org/10.3390/catal10040447
Lončar, N., Eryilmaz, J., Senel, E., Kaplan, G., Fraaije, M., & Cobanoglu, O. (2020). Process and apparatus for dyeing textiles. (Patent No. WO2020015839).
Martin, C., Trajkovic, M., & Fraaije, M. (2020). Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase. Angewandte Chemie (International ed. in English), 59(12), 4869-4872. https://doi.org/10.1002/anie.201914877
Fabara, A. N., & Fraaije, M. W. (2020). Production of indigo through the use of a dual-function substrate and a bifunctional fusion enzyme. Enzyme and Microbial Technology, 142, Article 109692. https://doi.org/10.1016/j.enzmictec.2020.109692
Nicoll, C. R., Bailleul, G., Fiorentini, F., Mascotti, M. L., Fraaije, M. W., & Mattevi, A. (2020). Publisher Correction: Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs (Nature Structural & Molecular Biology, (2020), 27, 1, (14-24), 10.1038/s41594-019-0347-2). Nature Structural & Molecular Biology, 27(2), 222. https://doi.org/10.1038/s41594-020-0378-8
Silveira, C. M., Moe, E., Fraaije, M., Martins, L. O., & Todorovic, S. (2020). Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases. RSC Advances, 10(19), 11095-11104. https://doi.org/10.1039/d0ra00950d
Lončar, N., Rozeboom, H. J., Franken, L. E., Stuart, M. C. A., & Fraaije, M. W. (2020). Structure of a robust bacterial protein cage and its application as a versatile biocatalytic platform through enzyme encapsulation. Biochemical and Biophysical Research Communications, 529(3), 548-553. Article j.bbrc.2020.06.059. https://doi.org/10.1016/j.bbrc.2020.06.059
Tong, Y., Trajkovic, M., Savino, S., van Berkel, W. J. H., & Fraaije, M. W. (2020). Substrate binding tunes the reactivity of hispidin 3-hydroxylase, a flavoprotein monooxygenase involved in fungal bioluminescence. The Journal of Biological Chemistry, 295(47), 16013-16022. https://doi.org/10.1074/jbc.RA120.014996
Martin, C., Binda, C., Fraaije, M. W., & Mattevi, A. (2020). The multipurpose family of flavoprotein oxidases. In P. Chaiyen, & F. Tamanoi (Eds.), Flavin-Dependent Enzymes : Mechanisms, Structures and Applications (Vol. 47, pp. 63-86). (The Enzymes). Elsevier. https://doi.org/10.1016/bs.enz.2020.05.002
Savino, S., & Fraaije, M. W. (2020). The vast repertoire of carbohydrate oxidases: An overview. Biotechnology Advances, 51, Article 107634. https://doi.org/10.1016/j.biotechadv.2020.107634
Niero, M., Righetto, I., Beneventi, E., de Laureto, P. P., Fraaije, M. W., Filippini, F., & Bergantino, E. (2020). Unique Features of a New Baeyer-Villiger Monooxygenase from a Halophilic Archaeon. Catalysts, 10(1), Article 128. https://doi.org/10.3390/catal10010128
Ewing, T. A., Gygli, G., Fraaije, M. W., & van Berkel, W. J. H. (2020). Vanillyl alcohol oxidase. In P. Chaiyen, & F. Tamanoi (Eds.), Flavin-Dependent Enzymes : Mechanisms, Structures and Applications (Vol. 47, pp. 87-116). (The Enzymes). Elsevier. https://doi.org/10.1016/bs.enz.2020.05.003

2019

Fabara, A. N., & Fraaije, M. W. (2020). An overview of microbial indigo-forming enzymes. Applied Microbiology and Biotechnology, 104(3), 925-933. https://doi.org/10.1007/s00253-019-10292-5
Maenpuen, S., Pongsupasa, V., Pensook, W., Anuwan, P., Kraivisitkul, N., Pinthong, C., Phonbuppha, J., Luanloet, T., Wijma, H. J., Fraaije, M. W., Lawan, N., Chaiyen, P., Wongnate, T., & Kraivisitkul, N. (2020). Creating Flavin Reductase Variants with Thermostable and Solvent‐Tolerant Properties by Rational‐Design Engineering. ChemBioChem, 21(10), 1481-1491. https://doi.org/10.1002/cbic.201900737
Nicoll, C. R., Bailleul, G., Fiorentini, F., Mascotti, M. L., Fraaije, M. W., & Mattevi, A. (2019). Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs. Nature Structural & Molecular Biology, 27(1), 14-24. https://doi.org/10.1038/s41594-019-0347-2
Furst, M. J. L. J., Gran-Scheuch, A., Aalbers, F. S., & Fraaije, M. W. (2019). Baeyer-Villiger Monooxygenases: Tunable Oxidative Biocatalysts. ACS Catalysis, 9(12), 11207-11241. https://doi.org/10.1021/acscatal.9b03396
Fürst, M. J. L. J., Fiorentini, F., & Fraaije, M. W. (2019). Beyond active site residues: overall structural dynamics control catalysis in flavin-containing and heme-containing monooxygenases. Current Opinion in Structural Biology, 59, 29-37. https://doi.org/10.1016/j.sbi.2019.01.019
Gandomkar, S., Jost, E., Loidolt, D., Swoboda, A., Pickl, M., Elaily, W., Daniel, B., Fraaije, M. W., Macheroux, P., & Kroutil, W. (2019). Biocatalytic Enantioselective Oxidation of Sec-Allylic Alcohols with Flavin-Dependent Oxidases. Advanced Synthesis & Catalysis, 361(22), 5264-5271. https://doi.org/10.1002/adsc.201900921
Habib, M. H., Rozeboom, H. J., & Fraaije, M. W. (2019). Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis. Molecules, 24(7), Article 1208. https://doi.org/10.3390/molecules24071208
Lončar, N., Fiorentini, F., Bailleul, G., Savino, S., Romero, E., Mattevi, A., & Fraaije, M. W. (2019). Characterization of a thermostable flavin-containing monooxygenase from Nitrincola lacisaponensis (NiFMO). Applied Microbiology and Biotechnology, 103(4), 1755-1764. https://doi.org/10.1007/s00253-018-09579-w
Drenth, J., Trajkovic, M., & Fraaije, M. W. (2019). Chemoenzymatic Synthesis of an Unnatural Deazaflavin Cofactor That Can Fuel F-420-Dependent Enzymes. ACS Catalysis, 9(7), 6435-6443. https://doi.org/10.1021/acscatal.9b01506
Huang, L., Aalbers, F. S., Tang, W., Röllig, R., Fraaije, M. W., & Kara, S. (2019). Convergent cascade catalyzed by monooxygenase - alcohol dehydrogenase fusion applied in organic media. ChemBioChem, 20(13), 1653-1658. https://doi.org/10.1002/cbic.201800814
Tischler, D., van Berkel, W. J. H., & Fraaije, M. W. (2019). Editorial: Actinobacteria, a Source of Biocatalytic Tools. Frontiers in Microbiology, 10, Article 800. https://doi.org/10.3389/fmicb.2019.00800
Fürst, M., Kerschbaumer, B., Rinnofner, C., Migglautsch, A., Winkler, M., & Fraaije, M. (2019). Exploring the Biocatalytic Potential of a Self-Sufficient Cytochr ome P450 from Thermothelomyces thermophila. Advanced Synthesis & Catalysis, 361(11), 2487–2496. https://doi.org/10.1002/adsc.201900076
Loncar, N., Draskovic, N., Bozic, N., Romero, E., Simic, S., Opsenica, I., Vujcic, Z., & Fraaije, M. W. (2019). Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts, 9(5), Article 463. https://doi.org/10.3390/catal9050463
Fraaije, M. W., Romero Guzman, E., Mattevi, A., & Nguyen, Q.-T. (2019). Mutant alcohol oxidases and use thereof in the conversion of diols and polyols. (Patent No. WO2019212351). https://worldwide.espacenet.com/publicationDetails/originalDocument?CC=WO&NR=2019212351A2&KC=A2&FT=D&ND=3&date=20191107&DB=&locale=en_EP
Fürst, M., Boonstra, M., Bandstra, S., & Fraaije, M. (2019). Stabilization of cyclohexanone monooxygenase by computational and experimental library design. Biotechnology and Bioengineering, 116(9), 2167-2177. https://doi.org/10.1002/bit.27022
Lončar, N., van Beek, H. L., & Fraaije, M. W. (2019). Structure-Based Redesign of a Self-Sufficient Flavin-Containing Monooxygenase towards Indigo Production. International Journal of Molecular Sciences, 20(24), Article 6148. https://doi.org/10.3390/ijms20246148
Mourelle-Insua, A., Aalbers, F. S., Lavandera, I., Gotor-Fernandez, V., & Fraaije, M. W. (2019). What to sacrifice? Fusions of cofactor regenerating enzymes with Baeyer-Villiger monooxygenases and alcohol dehydrogenases for self-sufficient redox biocatalysis. Tetrahedron, 75(13), 1832-1839. https://doi.org/10.1016/j.tet.2019.02.015

2018

Aalbers, F., & Fraaije, M. (2019). Design of artificial alcohol oxidases: alcohol dehydrogenase - NADPH oxidase fusions for continuous oxidations. ChemBioChem, 20(1), 51-56. Article cbic.201800421. https://doi.org/10.1002/cbic.201800421
Aalbers, F., & Fraaije, M. (2019). Enzyme fusions in biocatalysis: Coupling reactions by pairing enzymes. ChemBioChem, 20(1), 20-28. Article cbic.201800394. https://doi.org/10.1002/cbic.201800394
Ferrari, A. R., Rozeboom, H. J., Vugts, A. S. C., Koetsier, M. J., Floor, R., & Fraaije, M. W. (2018). Characterization of Two VAO-Type Flavoprotein Oxidases from Myceliophthora thermophila. Molecules, 23(1). https://doi.org/10.3390/molecules23010111
Martin, C., Ovalle Maqueo, A., Wijma, H. J., & Fraaije, M. W. (2018). Creating a more robust 5-hydroxymethylfurfural oxidase by combining computational predictions with a novel effective library design. Biotechnology for Biofuels, 11, 1-9. Article 56. https://doi.org/10.1186/s13068-018-1051-x
Mathew, S., Trajkovic, M., Kumar, H., Nguyen, Q.-T., & Fraaije, M. W. (2018). Enantio- and regioselective ene-reductions using F420H2-dependent enzymes. Chemical communications (Cambridge, England), 54(79), 11208-11211. Article C8CC04449J. https://doi.org/10.1039/c8cc04449j
Fürst, M., Martin, C., Lončar, N., & Fraaije, M. (2018). Experimental Protocols for Generating Focused Mutant Libraries and Screening for Thermostable Proteins. In N. Scrutton (Ed.), Enzymes in Synthetic Biology (pp. 151-187). (Methods in Enzymology; Vol. 608). Academic Press. https://doi.org/10.1016/bs.mie.2018.04.007
Pickl, M., Swoboda, A., Romero, E., Winkler, C., Binda, C., Mattevi, A., Faber, K., & Fraaije, M. (2018). Kinetic Resolution of sec-Thiols by Enantioselective Oxidation with Rationally Engineered 5-(Hydroxymethyl) furfural Oxidase. Angewandte Chemie - International Edition, 57(11), 2864-2868. Article anie.201713189. https://doi.org/10.1002/anie.201713189
Gran-Scheuch, A., Trajkovic, M., Parra, L., & Fraaije, M. W. (2018). Mining the Genome of: Two New Type I Baeyer-Villiger Monooxygenases From Atacama Desert. Frontiers in Microbiology, 9, Article 1609. https://doi.org/10.3389/fmicb.2018.01609
Li, G., Garcia-Borràs, M., Fürst, M., Ilie, A., Fraaije, M., Houk, K. N., & Reetz, M. T. (2018). Overriding Traditional Electronic Effects in Biocatalytic Baeyer-Villiger Reactions by Directed Evolution. Journal of the American Chemical Society, 140(33), 10464-10472. Article jacs.8b04742. https://doi.org/10.1021/jacs.8b04742
Mascotti, M. L., Kumar, H., Nguyen, Q.-T., Ayub, M. J., & Fraaije, M. W. (2018). Reconstructing the evolutionary history of F-420-dependent dehydrogenases. Scientific Reports, 8(1), Article 17571. https://doi.org/10.1038/s41598-018-35590-2
Romero, E., Gómez Castellanos, J. R., Gadda, G., Fraaije, M. W., & Mattevi, A. (2018). Same Substrate, Many Reactions: Oxygen Activation in Flavoenzymes. Chemical reviews, 118(4), 1742-1769. https://doi.org/10.1021/acs.chemrev.7b00650

2017

Beyer, N., Kulig, J. K., Fraaije, M. W., Hayes, M. A., & Janssen, D. B. (2018). Exploring PTDH-P450BM3 variants for the synthesis of drug metabolites. ChemBioChem, 19(4), 326-337. Article cbic.201700470. https://doi.org/10.1002/cbic.201700470
Delgove, M., Fürst, M., Fraaije, M., Bernaerts, K., & De Wildeman, S. M. A. (2018). Exploring the substrate scope of Baeyer-Villiger monooxygenases with branched lactones as entry towards polyesters. ChemBioChem, 19(4), 354-360. https://doi.org/10.1002/cbic.201700427
Burgener, S., Schwander, T., Romero, E., Fraaije, M. W., & Erb, T. J. (2018). Molecular Basis for Converting (2S)-Methylsuccinyl-CoA Dehydrogenase into an Oxidase. Molecules, 23(1), Article 68. https://doi.org/10.3390/molecules23010068
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