ReviewInternational journal of molecular sciences2012
Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.
Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 74 citations in OpenAlex.
- Structural Principles of Covalent Flavin Modification in Oxidoreductases.Biochemistry · 2026Review
- A Hooker Oxygenase Archetype in Polyketide Biosynthesis Challenging the Baeyer-Villiger Monooxygenase Paradigm.Journal of the American Chemical Society · 2026Article
- Functional analysis of R144 in the flavin oxidation mechanism of a flavin-dependent N-monooxygenase.Protein science : a publication of the Protein Society · 2025Article
- Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia.Acta crystallographica. Section F, Structural biology communications · 2023Article
- A flavin-monooxygenase catalyzing oxepinone formation and the complete biosynthesis of vibralactone.Nature communications · 2023Article
- Identification of novel coenzyme QThe Journal of biological chemistry · 2023Article
- Assigning function to active site residues ofFrontiers in molecular biosciences · 2023Article
- Comparing ultrafast excited state quenching of flavin 1,NPhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis.Angewandte Chemie (International ed. in English) · 2021Article
- Trapping conformational states of a flavin-dependentThe Journal of biological chemistry · 2020Article
- Photoinduced monooxygenation involving NAD(P)H-FAD sequential single-electron transfer.Nature communications · 2020Article
- Bioinformatic Analysis of the Flavin-Dependent Amine Oxidase Superfamily: Adaptations for Substrate Specificity and Catalytic Diversity.Journal of molecular biology · 2020Article
- Structural analyses of the Group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations.The Journal of biological chemistry · 2020Article
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- Comprehensive genomic analysis of an indigenous Pseudomonas pseudoalcaligenes degrading phenolic compounds.Scientific reports · 2019Article
- Structural basis for selectivity in flavin-dependent monooxygenase-catalyzed oxidative dearomatization.ACS catalysis · 2019Article
- Flavin oxidation in flavin-dependent N-monooxygenases.Protein science : a publication of the Protein Society · 2019Article
- Biodegradation of 7-Hydroxycoumarin inMolecules (Basel, Switzerland) · 2018Article
- PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis inThe Journal of biological chemistry · 2018Article
- Pyridine Nucleotide Coenzyme Specificity ofFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flavoprotein monooxygenases (FPMOs) exhibit an array of mechanistic solutions to a common chemical objective; the monooxygenation of a target substrate. Each FPMO efficiently couples reduction of a flavin cofactor by NAD(P)H to oxygenation of the target substrate via a (hydro)peroxyflavin intermediate. This purpose of this review is to describe in detail the Class A flavoprotein hydroxylases (FPMO) in the context of the other FPMO classes (B-F). Both one and two component FPMOs are found in nature. Two-component enzymes require, in addition to the monooxygenase, the involvement of a reductase that first catalyzes the reduction of the flavin by NAD(P)H. The Class A and B FPMOs are single-component and manage to orchestrate the same net reaction within a single peptide. The Class A enzymes have, by some considerable margin, the most complete research record. These enzymes use choreographed movements of the flavin ring that facilitate access of the organic substrates to the active site, provide a means for interaction of NADPH with the flavin, offer a mechanism to sequester the dioxygen reduction chemistry from solvent and a means to release the product. The majority of the discrete catalytic events of the catalytic cycle can be observed directly in exquisite detail using spectrophotometric kinetic methods and many of the key mechanistic conclusions are further supported by structural data. This review attempts to compile each of the key observations made for both paradigm and newly discovered examples of Class A FPMOs into a complete catalytic description of one enzymatic turnover.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.