ArticleJournal of the American Chemical Society2012
Evidence for oxygen binding at the active site of particulate methane monooxygenase.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 94 citations in OpenAlex.
- Discovery of a Copper-Binding Carbohydrate-Binding Module Regulating the Activity of Lytic Polysaccharide Monooxygenases.Journal of the American Chemical Society · 2025Article
- Critical evaluation of three cryo-EM structures of particulate methane monooxygenase by quantum refinement.Acta crystallographica. Section D, Structural biology · 2025Article
- Recent Advances in Bioinspired Cu-Directed C-H Hydroxylation Reactions.Accounts of chemical research · 2025Article
- Incorporating the Soil Gas Gradient Method and Functional Genes to Assess the Natural Source Zone Depletion at a Petroleum-Hydrocarbon-Contaminated Site of a Purification Plant in Northwest China.Life (Basel, Switzerland) · 2022Article
- Cu-promoted intramolecular hydroxylation of CH bonds using directing groups with varying denticity.Journal of inorganic biochemistry · 2021Article
- Particulate methane monooxygenase contains only mononuclear copper centers.Science (New York, N.Y.) · 2019Article
- Copper-Promoted Functionalization of Organic Molecules: from Biologically Relevant Cu/OChemical reviews · 2019Review
- Acid/base triggered interconversion of μ-ηChemical science · 2017Article
- A tale of two methane monooxygenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Substrate and Lewis Acid Coordination Promote O-O Bond Cleavage of an Unreactive LJournal of the American Chemical Society · 2017Article
- Copper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.Chemical reviews · 2017Review
- Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.Journal of the American Chemical Society · 2016Review
- Printable enzyme-embedded materials for methane to methanol conversion.Nature communications · 2016Article
- A Cu4S model for the nitrous oxide reductase active sites supported only by nitrogen ligands.Chemical communications (Cambridge, England) · 2015Article
- Enzymatic oxidation of methane.Biochemistry · 2015Review
- Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath).Biochemistry · 2014Article
- Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.Proteins · 2014Article
- Identification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterization.Journal of the American Chemical Society · 2014Article
- Effects of zinc on particulate methane monooxygenase activity and structure.The Journal of biological chemistry · 2014Article
- Hydroxo-bridged dicopper(II,III) and -(III,III) complexes: models for putative intermediates in oxidation catalysis.Journal of the American Chemical Society · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that converts methane to methanol in methanotrophic bacteria. The enzyme consists of three subunits, pmoB, pmoA, and pmoC, organized in an α(3)β(3)γ(3) trimer. Studies of intact pMMO and a recombinant soluble fragment of the pmoB subunit (denoted as spmoB) indicate that the active site is located within the soluble region of pmoB at the site of a crystallographically modeled dicopper center. In this work, we have investigated the reactivity of pMMO and spmoB with oxidants. Upon reduction and treatment of spmoB with O(2) or H(2)O(2) or pMMO with H(2)O(2), an absorbance feature at 345 nm is generated. The energy and intensity of this band are similar to those of the μ-η(2):η(2)-peroxo-Cu(II)(2) species formed in several dicopper enzymes and model compounds. The feature is not observed in inactive spmoB variants in which the dicopper center is disrupted, consistent with O(2) binding to the proposed active site. Reaction of the 345 nm species with CH(4) results in the disappearance of the spectroscopic feature, suggesting that this O(2) intermediate is mechanistically relevant. Taken together, these observations provide strong new support for the identity and location of the pMMO active site.
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