Baeyer− Villiger monooxygenases: more than just green chemistry

H Leisch, K Morley, PCK Lau - Chemical reviews, 2011 - ACS Publications
What is life without oxygen is a rhetorical question. On the other hand, unraveling the
intricacies and understanding the various mechanisms underpinning the biological …

The enigmatic reaction of flavins with oxygen

P Chaiyen, MW Fraaije, A Mattevi - Trends in biochemical sciences, 2012 - cell.com
The reaction of flavoenzymes with oxygen remains a fascinating area of research because
of its relevance for reactive oxygen species (ROS) generation. Several exciting recent …

Evolution of enzyme functionality in the flavin-containing monooxygenases

G Bailleul, G Yang, CR Nicoll, A Mattevi… - Nature …, 2023 - nature.com
Among the molecular mechanisms of adaptation in biology, enzyme functional
diversification is indispensable. By allowing organisms to expand their catalytic repertoires …

Heteroatom–heteroatom bond formation in natural product biosynthesis

AJ Waldman, TL Ng, P Wang, EP Balskus - Chemical reviews, 2017 - ACS Publications
Natural products that contain functional groups with heteroatom-heteroatom linkages (X–X,
where X= N, O, S, and P) are a small yet intriguing group of metabolites. The reactivity and …

Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs

CR Nicoll, G Bailleul, F Fiorentini, ML Mascotti… - Nature structural & …, 2020 - nature.com
Flavin-containing monooxygenases (FMOs) are ubiquitous in all domains of life and
metabolize a myriad of xenobiotics, including toxins, pesticides and drugs. However, despite …

Snapshots of enzymatic Baeyer-Villiger catalysis: oxygen activation and intermediate stabilization

R Orru, HM Dudek, C Martinoli, DET Pazmiño… - Journal of Biological …, 2011 - ASBMB
Baeyer-Villiger monooxygenases catalyze the oxidation of carbonylic substrates to ester or
lactone products using NADPH as electron donor and molecular oxygen as oxidative …

The substrate-bound crystal structure of a Baeyer–Villiger monooxygenase exhibits a Criegee-like conformation

BJ Yachnin, T Sprules, MB McEvoy… - Journal of the …, 2012 - ACS Publications
The Baeyer–Villiger monooxygenases (BVMOs) are a family of bacterial flavoproteins that
catalyze the synthetically useful Baeyer–Villiger oxidation reaction. This involves the …

Biocatalytic characterization of human FMO5: unearthing Baeyer–Villiger reactions in humans

F Fiorentini, M Geier, C Binda, M Winkler… - ACS chemical …, 2016 - ACS Publications
Flavin-containing mono-oxygenases are known as potent drug-metabolizing enzymes,
providing complementary functions to the well-investigated cytochrome P450 mono …

Proton-coupled electron transfer and adduct configuration are important for C4a-hydroperoxyflavin formation and stabilization in a flavoenzyme

T Wongnate, P Surawatanawong… - Journal of the …, 2014 - ACS Publications
Determination of the mechanism of dioxygen activation by flavoenzymes remains one of the
most challenging problems in flavoenzymology for which the underlying theoretical basis is …

Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases

S Franceschini, M Fedkenheuer, NJ Vogelaar… - Biochemistry, 2012 - ACS Publications
SidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N 5-
hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The …