ArticleThe Journal of biological chemistry2010
Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- Functional analysis of R144 in the flavin oxidation mechanism of a flavin-dependent N-monooxygenase.Protein science : a publication of the Protein Society · 2025Article
- Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The dynamics of the flavin, NADPH, and active site loops determine the mechanism of activation of class B flavin-dependent monooxygenases.Protein science : a publication of the Protein Society · 2024Article
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Flavin-dependent N-hydroxylating enzymes: distribution and application.Applied microbiology and biotechnology · 2020Review
- Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.Protein science : a publication of the Protein Society · 2020Article
- PvdF of pyoverdin biosynthesis is a structurally unique NArchives of biochemistry and biophysics · 2019Article
- Flavin oxidation in flavin-dependent N-monooxygenases.Protein science : a publication of the Protein Society · 2019Article
- Unique Biochemical and Sequence Features Enable BluB To Destroy Flavin and Distinguish BluB from the Flavin Monooxygenase Superfamily.Biochemistry · 2018Article
- Characterization of the flavoenzyme XiaK as anChemical science · 2017Article
- Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Chemical reviews · 2017Review
- Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.The Journal of biological chemistry · 2017Article
- Mechanism of Rifampicin Inactivation in Nocardia farcinica.PloS one · 2016Article
- An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.The Journal of biological chemistry · 2015Article
- Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase.Biochemistry · 2014Article
- How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase.Biochemistry · 2014Article
- Auxin biosynthesis.The arabidopsis book · 2014Article
- The reaction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1 provide an understanding of the para-hydroxylation enzyme catalytic cycle.The Journal of biological chemistry · 2013Article
- Role of Ser-257 in the sliding mechanism of NADP(H) in the reaction catalyzed by the Aspergillus fumigatus flavin-dependent ornithine N5-monooxygenase SidA.The Journal of biological chemistry · 2013Article
- The biochemical mechanism of auxin biosynthesis by an arabidopsis YUCCA flavin-containing monooxygenase.The Journal of biological chemistry · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Many siderophores used for the uptake and intracellular storage of essential iron contain hydroxamate chelating groups. Their biosyntheses are typically initiated by hydroxylation of the primary amine side chains of l-ornithine or l-lysine. This reaction is catalyzed by members of a widespread family of FAD-dependent monooxygenases. Here the kinetic mechanism for a representative family member has been extensively characterized by steady state and transient kinetic methods, using heterologously expressed N(5)-l-ornithine monooxygenase from the pathogenic fungus Aspergillus fumigatus. Spectroscopic data and kinetic analyses suggest a model in which a molecule of hydroxylatable substrate serves as an activator for the reaction of the reduced flavin and O(2). The rate acceleration is only ∼5-fold, a mild effect of substrate on formation of the C4a-hydroperoxide that does not influence the overall rate of turnover. The effect is also observed with the bacterial ornithine monooxygenase PvdA. The C4a-hydroperoxide is stabilized in the absence of hydroxylatable substrate by the presence of bound NADP(+) (t(½) = 33 min, 25 °C, pH 8). NADP(+) therefore is a likely regulator of O(2) and substrate reactivity in the siderophore-associated monooxygenases. Aside from the activating effect of the hydroxylatable substrate, the siderophore-associated monooxygenases share a kinetic mechanism with the hepatic microsomal flavin monooxygenases and bacterial Baeyer-Villiger monooxygenases, with which they share only moderate sequence homology and from which they are distinguished by their acute substrate specificity. The remarkable specificity of the N(5)-l-ornithine monooxygenase-catalyzed reaction suggests added means of reaction control beyond those documented in related well characterized flavoenzymes.
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