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Fraaije, Prof. Marco

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.

2021

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, [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, [108888]. https://doi.org/10.1016/j.abb.2021.108888
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
Fraaije, M. W., Trajkovic, M., & Martin, C. (2021). Means and methods for selective double diol oxidation. (Patent No. WO2021071356).
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), [905]. https://doi.org/10.3390/biom11060905
Mascotti, M. L., Juri Ayub, M., & Fraaije, M. W. (2021). On the diversity of F420 -dependent oxidoreductases: A sequence- and structure-based classification. Proteins, [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), [7998]. https://doi.org/10.3390/ijms22157998
Gran-Scheuch, A., Parra, L., & Fraaije, M. W. (2021). Systematic Assessment of Uncoupling in Flavoprotein Oxidases and Monooxygenases. ACS Sustainable Chemistry and Engineering. https://doi.org/10.1021/acssuschemeng.1c02012

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, [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. [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. [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, [ 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. [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), [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, [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. [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, [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), [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), [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, [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), [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), [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. [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. [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. [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. [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. [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, [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. [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), [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
Fürst, M., Romero Guzman, E., Gómez Castellanos, J. R., Fraaije, M., & Mattevi, A. (2018). Side-Chain Pruning Has Limited Impact on Substrate Preference in a Promiscuous Enzyme. ACS Catalysis, 8(12), 11648-11656. https://doi.org/10.1021/acscatal.8b03793
Nguyen, Q-T., Romero, E., Dijkman, W., de Vasconcellos, S. P., Binda, C., Mattevi, A., & Fraaije, M. W. (2018). Structure-based engineering of Phanerochaete chrysosporium alcohol oxidase for enhanced oxidative power towards glycerol. Biochemistry, 57(43), 6209-6218. https://doi.org/10.1021/acs.biochem.8b00918
Habib, M., Trajkovic, M., & Fraaije, M. W. (2018). The Biocatalytic Synthesis of Syringaresinol from 2,6-Dimethoxy-4-allylphenol in One-Pot Using a Tailored Oxidase/Peroxidase System. ACS Catalysis, 8(6), 5549-5552. https://doi.org/10.1021/acscatal.8b01235

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. [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), [68]. https://doi.org/10.3390/molecules23010068
Habib, M. H. M., Deuss, P. J., Loncar, N., Trajkovic, M., & Fraaije, M. W. (2017). A Biocatalytic One-Pot Approach for the Preparation of Lignin Oligomers Using an Oxidase/Peroxidase Cascade Enzyme System. Advanced Synthesis & Catalysis, 359(19), 3354-3361. https://doi.org/10.1002/adsc.201700650
Fiorentini, F., Romero, E., Fraaije, M. W., Faber, K., Hall, M., & Mattevi, A. (2017). Baeyer-Villiger Monooxygenase FMO5 as Entry Point in Drug Metabolism. ACS chemical biology, 12(9), 2379-2387. https://doi.org/10.1021/acschembio.7b00470
Kumar, H., & Fraaije, M. (2017). Conversion of Furans by Baeyer-Villiger Monooxygenases. Catalysts, 7(6), [179]. https://doi.org/10.3390/catal7060179
Aalbers, F. S., & Fraaije, M. W. (2017). Coupled reactions by coupled enzymes: alcohol to lactone cascade with alcohol dehydrogenase-cyclohexanone monooxygenase fusions. Applied Microbiology and Biotechnology, 20(101), 7557-7565. https://doi.org/10.1007/s00253-017-8501-4
Colpa, D. I., Loncar, N., Schmidt, M., & Fraaije, M. (2017). Creating peroxidase-oxidase fusion enzymes as toolbox for cascade reactions. ChemBioChem, 18, 2226-2230. [cbic.201700478]. https://doi.org/10.1002/cbic.201700478
Magnani, F., Nenci, S., Fananas, E. M., Ceccon, M., Romero, E., Fraaije, M. W., & Mattevi, A. (2017). Crystal structures and atomic model of NADPH oxidase. Proceedings of the National Academy of Science of the United States of America, 114(26), 6764-6769. https://doi.org/10.1073/pnas.1702293114
van Beek, H. L., Romero, E., & Fraaije, M. W. (2017). Engineering Cyclohexanone Monooxygenase for the Production of Methyl Propanoate. ACS chemical biology, 12(1), 291-299. [acschembio.6b00965]. https://doi.org/10.1021/acschembio.6b00965
Nguyen, Q. T., Mattevi, A., & Fraaije, M. W. (2017). Expanding the Repertoire of Flavoenzyme-Based Biocatalysis. In T. Matsuda (Ed.), Future Directions in Biocatalysis: Second Edition (2nd ed., pp. 119-133). Elsevier. https://doi.org/10.1016/B978-0-444-63743-7.00006-8
Oberleitner, N., Ressmann, A. K., Bica, K., Gaertner, P., Fraaije, M. W., Bornscheuer, U. T., Rudroff, F., & Mihovilovic, M. D. (2017). From waste to value - direct utilization of limonene from orange peel in a biocatalytic cascade reaction towards chiral carvolactone. Green Chemistry, 19(2), 367-371. https://doi.org/10.1039/c6gc01138a
Kumar, H., Nguyen, Q-T., Binda, C., Mattevi, A., & Fraaije, M. W. (2017). Isolation and characterization of a thermostable F420:NADPH oxidoreductase from Thermobifida fusca. The Journal of Biological Chemistry, 292, 10123-10130. [jbc.M117.787754]. https://doi.org/10.1074/jbc.M117.787754
Li, G., Fürst, M. J. L. J., Mansouri, H. R., Ressmann, A. K., Ilie, A., Rudroff, F., Mihovilovic, M. D., Fraaije, M. W., & Reetz, M. T. (2017). Manipulating the stereoselectivity of the thermostable Baeyer-Villiger monooxygenase TmCHMO by directed evolution. Organic & Biomolecular Chemistry, 15, 9824-9829. https://doi.org/10.1039/c7ob02692g
Huang, L., Romero, E., Ressmann, A. K., Rudroff, F., Hollmann, F., Fraaije, M. W., & Kara, S. (2017). Nicotinamide Adenine Dinucleotide-Dependent Redox-Neutral Convergent Cascade for Lactonizations with Type II Flavin-Containing Monooxygenase. Advanced Synthesis & Catalysis, 359(12), 2142-2148. https://doi.org/10.1002/adsc.201700401
Fürst, M. J. L. J., Savino, S., Dudek, H. M., Gómez Castellanos, J. R., Gutiérrez de Souza, C., Rovida, S., Fraaije, M. W., & Mattevi, A. (2017). Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila: A Structurally Distinct Biocatalyst for Bulky Substrates. Journal of the American Chemical Society, 139(2), 627-630. https://doi.org/10.1021/jacs.6b12246
de Gonzalo, G., Fürst, M., & Fraaije, M. (2017). Polycyclic Ketone Monooxygenase (PockeMO): A Robust Biocatalyst for the Synthesis of Optically Active Sulfoxides. Catalysts, 7(10), 1-10. [288]. https://doi.org/10.3390/catal7100288
Pickl, M., Winkler, C. K., Glueck, S. M., Fraaije, M. W., & Faber, K. (2017). Rational Engineering of a Flavoprotein Oxidase for Improved Direct Oxidation of Alcohols to Carboxylic Acids. Molecules, 22(12), 1-8. [2205]. https://doi.org/10.3390/molecules22122205
Ewing, T. A., Fraaije, M. W., Mattevi, A., & van Berkel, W. J. H. (2017). The VAO/PCMH flavoprotein family. Archives of Biochemistry and Biophysics, 632, 104-117. https://doi.org/10.1016/j.abb.2017.06.022
Ewing, T. A., Nguyen, Q-T., Allan, R. C., Gygli, G., Romero, E., Binda, C., Fraaije, M. W., Mattevi, A., & van Berkel, W. J. H. (2017). Two tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase. The Journal of Biological Chemistry, 292(35), 14668-14679. https://doi.org/10.1074/jbc.M117.778449

2016

Nguyen, Q-T., Trinco, G., Binda, C., Mattevi, A., & Fraaije, M. W. (2017). Discovery and characterization of an F420-dependent glucose-6-phosphate dehydrogenase (Rh-FGD1) from Rhodococcus jostii RHA1. Applied Microbiology and Biotechnology, 101(7), 2831-2842. https://doi.org/10.1007/s00253-016-8038-y
Beyer, N., Kulig, J. K., Bartsch, A., Hayes, M. A., Janssen, D. B., & Fraaije, M. W. (2017). P450BM3 fused to phosphite dehydrogenase allows phosphite-driven selective oxidations. Applied Microbiology and Biotechnology, 101, 2319-2331. https://doi.org/10.1007/s00253-016-7993-7
de Gonzalo, G., Colpa, D. I., Habib, M. H. M., & Fraaije, M. W. (2016). Bacterial enzymes involved in lignin degradation. Journal of Biotechnology, 236, 110-119. https://doi.org/10.1016/j.jbiotec.2016.08.011
Nguyen, Q-T., De Gonzalo, G., Binda, C., Rioz, A., Mattevi, A., & Fraaije, M. (2016). Biocatalytic properties and structural analysis of eugenol oxidase from Rhodococcus jostii RHA1: a versatile oxidative biocatalyst. ChemBioChem, 17(14), 1359-1366. [201600148]. https://doi.org/10.1002/cbic.201600148
Romero, E., Castellanos, J. R. G., Mattevi, A., & Fraaije, M. W. (2016). Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase. Angewandte Chemie - International Edition, 55(51), 15852-15855. [angie.201608951]. https://doi.org/10.1002/anie.201608951
Gaber, Y., Mekasha, S., Vaaje-Kolstad, G., Eijsink, V. G. H., & Fraaije, M. W. (2016). Characterization of a chitinase from the cellulolytic actinomycete Thermobifida fusca. Biochimica et biophysica acta-Proteins and proteomics, 1864(9), 1253-1259. https://doi.org/10.1016/j.bbapap.2016.04.010
Krzek, M., van Beek, H. L., Permentier, H. P., Bischoff, R., & Fraaije, M. W. (2016). Covalent immobilization of a flavoprotein monooxygenase via its flavin cofactor. Enzyme and Microbial Technology, 82, 138-143. https://doi.org/10.1016/j.enzmictec.2015.09.006
Ferrari, A. R., Rozeboom, H. J., Dobruchowska, J. M., van Leeuwen, S. S., Vugts, A. S. C., Koetsier, M. J., Visser, J., & Fraaije, M. W. (2016). Discovery of a xylooligosaccharide oxidase from Myceliophthora thermophila C1. The Journal of Biological Chemistry, 291(45), 23709-23718. [jbc.M116.741173]. https://doi.org/10.1074/jbc.M116.741173
Loncar, N., Colpa, D. I., & Fraaije, M. W. (2016). Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. Tetrahedron, 72(46), 7276-7281. https://doi.org/10.1016/j.tet.2015.12.078
Colpa, D. I., & Fraaije, M. W. (2016). High overexpression of dye decolorizing peroxidase TfuDyP leads to the incorporation of heme precursor protoporphyrin IX. Journal of Molecular Catalysis B: Enzymatic, 134(Part B), 372-377. https://doi.org/10.1016/j.molcatb.2016.08.017
Groeneveld, M., van Beek, H. L., Duetz, W. A., & Fraaije, M. W. (2016). Identification of a novel oxygenase capable of regiospecific hydroxylation of D-limonene into (+)-trans-carveol. Tetrahedron, 72(46), 7263-7267. https://doi.org/10.1016/j.tet.2015.12.061
Gul, T., Krzek, M., Permentier, H., Fraaije, M., & Bischoff, R. (2016). Microbial Flavoprotein Monooxygenases as Mimics of Mammalian Flavin-Containing Monooxygenases for the Enantioselective Preparation of Drug Metabolites. Drug Metabolism and Disposition, 44(8), 1270-1276. https://doi.org/10.1124/dmd.115.069104
Brondani, P. B., Fraaije, M. W., & Gonzalo, G. D. (2016). Recent Developments in Flavin-Based Catalysis: Enzymatic Sulfoxidation. In R. N. Patel (Ed.), Green Biocatalysis (pp. 149-164). Wiley. https://doi.org/10.1002/9781118828083.ch6
van Berkel, W., Fraaije, M., & Hollmann, F. (2016). Special issue OxiZymes 2016. Journal of Molecular Catalysis B: Enzymatic, 134(Part B), 273-273. https://doi.org/10.1016/j.molcatb.2016.11.009

2015

de Gonzalo, G., van Berkel, W. J. H., & Fraaije, M. (2015). Baeyer-Villiger oxidations. In K. Faber, W-D. Fessner, & N. J. Turner (Eds.), Science of Synthesis: Biocatalysis in Organic Synthesis (Vol. 3, pp. 187-234). Thieme.
Lončar, N., & Fraaije, M. W. (2015). Catalases as biocatalysts in technical applications: current state and perspectives. Applied Microbiology and Biotechnology, 99(8), 3351-3357. https://doi.org/10.1007/s00253-015-6512-6
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