Fraaije, prof. dr. Marco
Prof. dr. ir. Marco W. Fraaije studeerde Moleculaire Wetenschappen aan de Universiteit van Wageningen, waar hij ook promoveerde. Hij was postdoctoraal onderzoeker bij het departement Genetics & Microbiology aan de Universiteit van Pavia (Italië) en is sinds 1999 werkzaam bij de Rijksuniversiteit Groningen. Als assistent-professor leidde hij verschillende onderzoeken gericht op het ontdekken van nieuwe biokatalysatoren (enzymen) en het onderzoeken van hun functie. Tegenwoordig is hij werkzaam als hoogleraar in moleculaire enzymologie. In 2016 werd hem een Vici-onderzoeksbeurs toegekend en in 2018 ontving hij de BIOCAT Science Award voor zijn academische bijdrage aan het onderzoeksveld van de biotechnologie. Fraaije publiceerde honderden artikelen, maar richtte zich vooral op biokatalyse en enzyme engineering. Zijn onderzoek centreert zich rond het ontdekken, herontwerpen en toepassen van nieuwe enzymen met de nadruk op flavine-afhankelijke enzymen, enzymen die gebruik maken van vitamine B2 voor hun functie.
ROBOX (Expanding the industrial use of Robust Oxidative Biocatalysts)
Naast de academische toepassingen van zijn onderzoeken slaat Fraaije ook een brug tussen de wetenschappelijke wereld en de industrie. Zo was hij medeoprichter en nu adviseur van het start-up bedrijf GECCO-biotech. Ook coördineerde hij meerdere EU-gefinancierde initiatieven, waaronder het ROBOX project. Dit project was voornamelijk gericht op het ontwerpen van robuuste enzymen die gebruikt kunnen worden in oxidatieprocessen. Deze enzymen kunnen chemische reacties vervangen die momenteel worden ingezet in productieprocessen, met als doel de behoefte aan het gebruik van edelmetalen en gifstoffen te verminderen. Daarnaast werkt de onderzoeksgroep aan computer-gebaseerde engineering methoden om enzymen snel aan te kunnen passen voor biotechnologische toepassingen.
Eerder in het nieuws
Contact en meer informatie
Publicaties
2024
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. Advance online
publication. https://doi.org/10.1021/acssynbio.3c00718
Russo,
S., Prats Luján, A., Fraaije,
M., & Poelarends, G. J. (2024).
Synthesis of Pharmaceutically Relevant Arylamines Enabled by
a Nitroreductase from Bacillus tequilensis.
ChemBioChem, Article e202300846. Advance
online publication. https://doi.org/10.1002/cbic.202300846
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
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