ArticleThe Journal of biological chemistry2011
Snapshots of enzymatic Baeyer-Villiger catalysis: oxygen activation and intermediate stabilization.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 128 citations in OpenAlex.
- The FAD-Dependent Monooxygenase Albo65 Mediates Self-Resistance in Albofungin Biosynthesis.JACS Au · 2026Article
- Mapping the effects of specific radiation damage and solvent radiolysis in buffers and crystals with online UV-Vis absorption spectroscopy.Acta crystallographica. Section D, Structural biology · 2026Article
- TheJournal of applied crystallography · 2025Article
- Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- A biosynthetic aspartate N-hydroxylase performs successive oxidations by holding intermediates at a site away from the catalytic center.The Journal of biological chemistry · 2023Article
- Structural basis of the stereoselective formation of the spirooxindole ring in the biosynthesis of citrinadins.Nature communications · 2021Article
- A Baeyer-Villiger monooxygenase from Cupriavidus basilensis catalyzes asymmetric synthesis of (R)-lansoprazole and other pharmaco-sulfoxides.Applied microbiology and biotechnology · 2021Article
- Investigation of a New Type I Baeyer-Villiger Monooxygenase from Amycolatopsis thermoflava Revealed High Thermodynamic but Limited Kinetic Stability.Chembiochem : a European journal of chemical biology · 2020Article
- An overview of microbial indigo-forming enzymes.Applied microbiology and biotechnology · 2020Review
- Morpholine-based buffers activate aerobic photobiocatalysisCatalysis science & technology · 2019Article
- Enzyme Fusions in Biocatalysis: Coupling Reactions by Pairing Enzymes.Chembiochem : a European journal of chemical biology · 2019Review
- Side-Chain Pruning Has Limited Impact on Substrate Preference in a Promiscuous Enzyme.ACS catalysis · 2018Article
- Improving catalytic activity of the Baeyer-Villiger monooxygenase-based Escherichia coli biocatalysts for the overproduction of (Z)-11-(heptanoyloxy)undec-9-enoic acid from ricinoleic acid.Scientific reports · 2018Article
- Reply to the Comment by Littlechild and Isupov.Microorganisms · 2017Article
- Prospecting Biotechnologically-Relevant Monooxygenases from Cold Sediment Metagenomes: An In Silico Approach.Marine drugs · 2017Article
- Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.The Journal of biological chemistry · 2017Article
- Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase.Angewandte Chemie (International ed. in English) · 2016Article
- Substitution of a Single Amino Acid Reverses the Regiospecificity of the Baeyer-Villiger Monooxygenase PntE in the Biosynthesis of the Antibiotic Pentalenolactone.Biochemistry · 2016Article
- The Oxygen Dilemma: A Severe Challenge for the Application of Monooxygenases?Chembiochem : a European journal of chemical biology · 2016Review
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Baeyer-Villiger monooxygenases catalyze the oxidation of carbonylic substrates to ester or lactone products using NADPH as electron donor and molecular oxygen as oxidative reactant. Using protein engineering, kinetics, microspectrophotometry, crystallography, and intermediate analogs, we have captured several snapshots along the catalytic cycle which highlight key features in enzyme catalysis. After acting as electron donor, the enzyme-bound NADP(H) forms an H-bond with the flavin cofactor. This interaction is critical for stabilizing the oxygen-activating flavin-peroxide intermediate that results from the reaction of the reduced cofactor with oxygen. An essential active-site arginine acts as anchoring element for proper binding of the ketone substrate. Its positively charged guanidinium group can enhance the propensity of the substrate to undergo a nucleophilic attack by the flavin-peroxide intermediate. Furthermore, the arginine side chain, together with the NADP(+) ribose group, forms the niche that hosts the negatively charged Criegee intermediate that is generated upon reaction of the substrate with the flavin-peroxide. The fascinating ability of Baeyer-Villiger monooxygenases to catalyze a complex multistep catalytic reaction originates from concerted action of this Arg-NADP(H) pair and the flavin subsequently to promote flavin reduction, oxygen activation, tetrahedral intermediate formation, and product synthesis and release. The emerging picture is that these enzymes are mainly oxygen-activating and "Criegee-stabilizing" catalysts that act on any chemically suitable substrate that can diffuse into the active site, emphasizing their potential value as toolboxes for biocatalytic applications.
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