ArticleBiochemistry2009
Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026Review
- Direct Methane to Methanol Conversion: An Overview of Non-Syn Gas Catalytic Strategies.Chemical record (New York, N.Y.) · 2025Review
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Electron Transfer to Hydroxylase through Component Interactions in Soluble Methane Monooxygenase.Journal of microbiology and biotechnology · 2022Article
- Generation of a μ-1,2-hydroperoxo FeNature communications · 2022Article
- X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics.Biochemistry · 2022Article
- Soluble Methane Monooxygenase Component Interactions Monitored byBiochemistry · 2021Article
- Structure-Spectroscopy Correlations for Intermediate Q of Soluble Methane Monooxygenase: Insights from QM/MM Calculations.Journal of the American Chemical Society · 2021Article
- Biochemistry of aerobic biological methane oxidation.Chemical Society reviews · 2021Review
- Structure and assembly of the diiron cofactor in the heme-oxygenase-like domain of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- High-Resolution XFEL Structure of the Soluble Methane Monooxygenase Hydroxylase Complex with its Regulatory Component at Ambient Temperature in Two Oxidation States.Journal of the American Chemical Society · 2020Article
- Structural Studies of theBiochemistry · 2020Article
- A Peroxodiiron(III/III) Intermediate Mediating BothJournal of the American Chemical Society · 2020Article
- ScJournal of the American Chemical Society · 2020Article
- Activation of a Non-Heme FeAngewandte Chemie (International ed. in English) · 2019Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells.The Journal of biological chemistry · 2017Review
- Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF.Journal of the American Chemical Society · 2017Article
- A tale of two methane monooxygenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Biocatalysts for methane conversion: big progress on breaking a small substrate.Current opinion in chemical biology · 2016Review
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2 authors.
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Abstract
Stopped-flow kinetic investigations of soluble methane monooxygenase (sMMO) from M. capsulatus (Bath) have clarified discrepancies that exist in the literature regarding several aspects of catalysis by this enzyme. The development of thorough kinetic analytical techniques has led to the discovery of two novel oxygenated iron species that accumulate in addition to the well-established intermediates H(peroxo) and Q. The first intermediate, P*, is a precursor to H(peroxo) and was identified when the reaction of reduced MMOH and MMOB with O(2) was carried out in the presence of >or=540 microM methane to suppress the dominating absorbance signal due to Q. The optical properties of P* are similar to those of H(peroxo), with epsilon(420) = 3500 M(-1) cm(-1) and epsilon(720) = 1250 M(-1) cm(-1). These values are suggestive of a peroxo-to-iron(III) charge-transfer transition and resemble those of peroxodiiron(III) intermediates characterized in other carboxylate-bridged diiron proteins and synthetic model complexes. The second identified intermediate, Q*, forms on the pathway of Q decay when reactions are performed in the absence of hydrocarbon substrate. Q* does not react with methane, forms independently of buffer composition, and displays a unique shoulder at 455 nm in its optical spectrum. Studies conducted at different pH values reveal that rate constants corresponding to P* decay/H(peroxo) formation and H(peroxo) decay/Q formation are both significantly retarded at high pH and indicate that both events require proton transfer. The processes exhibit normal kinetic solvent isotope effects (KSIEs) of 2.0 and 1.8, respectively, when the reactions are performed in D(2)O. Mechanisms are proposed to account for the observations of these novel intermediates and the proton dependencies of P* to H(peroxo) and H(peroxo) to Q conversion.
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