ArticleBiochemistry2010
Oxidation reactions performed by soluble methane monooxygenase hydroxylase intermediates H(peroxo) and Q proceed by distinct mechanisms.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 66 citations in OpenAlex.
- Cryo-EM Structures Reveal the Molecular Basis of Asymmetric Allosteric Activation by MMOB in the Hydroxylase of Soluble Methane Monooxygenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Nature of the Reactive Biferric Peroxy Intermediate P' in the Arylamine Oxygenases and Related Binuclear Fe Enzymes.Journal of the American Chemical Society · 2025Article
- The effect of lanthanum on growth and gene expression in a facultative methanotroph.Environmental microbiology · 2022Article
- X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics.Biochemistry · 2022Article
- BesC Initiates C-C Cleavage through a Substrate-Triggered and Reactive Diferric-Peroxo Intermediate.Journal of the American Chemical Society · 2021Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Journal of the American Chemical Society · 2017Article
- VTST/MT studies of the catalytic mechanism of C-H activation by transition metal complexes with [CuJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- A tale of two methane monooxygenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- A Peroxynitrite Dicopper Complex: Formation via Cu-NO and Cu-OJournal of the American Chemical Society · 2016Article
- Structure/function correlations over binuclear non-heme iron active sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.Journal of the American Chemical Society · 2016Review
- Mechanism for Six-Electron Aryl-N-Oxygenation by the Non-Heme Diiron Enzyme CmlI.Journal of the American Chemical Society · 2016Article
- Isolation and characterization of a dihydroxo-bridged iron(III,III)(μ-OH)2 diamond core derived from dioxygen.Inorganic chemistry · 2013Article
- Nuclear resonance vibrational spectroscopic and computational study of high-valent diiron complexes relevant to enzyme intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylase.Biochemistry · 2011Article
- Dioxygen activation in soluble methane monooxygenase.Accounts of chemical research · 2011Review
- Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.Biochemistry · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Soluble methane monooxygenase is a bacterial enzyme that converts methane to methanol at a carboxylate-bridged diiron center with exquisite control. Because the oxidizing power required for this transformation is demanding, it is not surprising that the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane. In this work we took advantage of this promiscuity of the enzyme to gain insight into the mechanisms of action of H(peroxo) and Q, two oxidants that are generated sequentially during the reaction of reduced protein with O(2). Using double-mixing stopped-flow spectroscopy, we investigated the reactions of the two intermediate species with a panel of substrates of varying C-H bond strength. Three classes of substrates were identified according to the rate-determining step in the reaction. We show for the first time that an inverse trend exists between the rate constant of reaction with H(peroxo) and the C-H bond strength of the hydrocarbon examined for those substrates in which C-H bond activation is rate-determining. Deuterium kinetic isotope effects revealed that reactions performed by Q, but probably not H(peroxo), involve extensive quantum mechanical tunneling. This difference sheds light on the observation that H(peroxo) is not a sufficiently potent oxidant to hydroxylate methane, whereas Q can perform this reaction in a facile manner. In addition, the reaction of H(peroxo) with acetonitrile appears to proceed by a distinct mechanism in which a cyanomethide anionic intermediate is generated, bolstering the argument that H(peroxo) is an electrophilic oxidant that operates via two-electron transfer chemistry.
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