ArticleNature chemical biology2020
Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 72 citations in OpenAlex.
- Structural Principles of Covalent Flavin Modification in Oxidoreductases.Biochemistry · 2026Review
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- Structural Basis of Sequential Enantioselective Epoxidation by a Flavin-Dependent Monooxygenase in Lasalocid A Biosynthesis.Angewandte Chemie (International ed. in English) · 2025Article
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- Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.Angewandte Chemie (International ed. in English) · 2024Article
- Structural, biophysical, and biochemical insights into C-S bond cleavage by dimethylsulfone monooxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- DszA Catalyzes C-S Bond Cleavage through NJournal of chemical information and modeling · 2024Article
- Biosynthesis of the bacterial antibiotic 3,7-dihydroxytropolone through enzymatic salvaging of catabolic shunt products.Chemical science · 2024Article
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Alkylcysteine Sulfoxide C-S Monooxygenase Uses a Flavin-Dependent Pummerer Rearrangement.Journal of the American Chemical Society · 2023Article
- Spin-Forbidden Addition of Molecular Oxygen to Stable Enol Intermediates-Decarboxylation of 2-Methyl-1-tetralone-2-carboxylic Acid.International journal of molecular sciences · 2023Article
- QM/MM Modeling of the Flavin Functionalization in the RutA Monooxygenase.Molecules (Basel, Switzerland) · 2023Article
- An acetyltransferase controls the metabolic flux in rubromycin polyketide biosynthesis by direct modulation of redox tailoring enzymes.Chemical science · 2022Article
- Three Rings to Rule Them All: How Versatile Flavoenzymes Orchestrate the Structural Diversification of Natural Products.Biochemistry · 2022Article
- Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis.Angewandte Chemie (International ed. in English) · 2021Article
- The Unexplored Importance of Fleeting Chiral Intermediates in Enzyme-Catalyzed Reactions.Journal of the American Chemical Society · 2021Article
- A Flavoprotein Dioxygenase Steers Bacterial Tropone Biosynthesis via Coenzyme A-Ester Oxygenolysis and Ring Epoxidation.Journal of the American Chemical Society · 2021Article
- Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer.The Journal of biological chemistry · 2021Article
- Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides.Nature communications · 2021Article
- Hexachlorobenzene Monooxygenase Substrate Selectivity and Catalysis: Structural and Biochemical Insights.Applied and environmental microbiology · 2020Article
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6 authors at 3 institutions in 2 countries.
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Abstract
One of the hallmark reactions catalyzed by flavin-dependent enzymes is the incorporation of an oxygen atom derived from dioxygen into organic substrates. For many decades, these flavin monooxygenases were assumed to use exclusively the flavin-C4a-(hydro)peroxide as their oxygen-transferring intermediate. We demonstrate that flavoenzymes may instead employ a flavin-N5-peroxide as a soft α-nucleophile for catalysis, which enables chemistry not accessible to canonical monooxygenases. This includes, for example, the redox-neutral cleavage of carbon-hetero bonds or the dehalogenation of inert environmental pollutants via atypical oxygenations. We furthermore identify a shared structural motif for dioxygen activation and N5-functionalization, suggesting a conserved pathway that may be operative in numerous characterized and uncharacterized flavoenzymes from diverse organisms. Our findings show that overlooked flavin-N5-oxygen adducts are more widespread and may facilitate versatile chemistry, thus upending the notion that flavin monooxygenases exclusively function as nature's equivalents to organic peroxides in synthetic chemistry.
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