ArticleBiochemistry2011
Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 154 citations in OpenAlex.
- Bisulfate-mediated selective methane oxidation under mild aqueous conditions.Science advances · 2026Article
- HChemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- Regulatory mechanisms of CHFrontiers in microbiology · 2026Article
- Structural insights into the catalytic mechanism of ammonia monooxygenase.Nature communications · 2025Article
- Critical evaluation of three cryo-EM structures of particulate methane monooxygenase by quantum refinement.Acta crystallographica. Section D, Structural biology · 2025Article
- Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.Nature communications · 2025Article
- Direct Methane to Methanol Conversion: An Overview of Non-Syn Gas Catalytic Strategies.Chemical record (New York, N.Y.) · 2025Review
- Structures of methane and ammonia monooxygenases in native membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanisms for Methane and Ammonia Oxidation by Particulate Methane Monooxygenase.The journal of physical chemistry. B · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Gene Stacking and Stoichiometric Expression of ER-Targeted Constructs Using "2A" Self-Cleaving Peptides.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Product analog binding identifies the copper active site of particulate methane monooxygenase.Nature catalysis · 2023Article
- Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants.Scientific reports · 2023Article
- Unexpected complexity of the ammonia monooxygenase in archaea.The ISME journal · 2023Article
- Cell-Free Protein Synthesis of Particulate Methane Monooxygenase into Nanodiscs.ACS synthetic biology · 2022Article
- Article
- Recent Insights into Cu-Based Catalytic Sites for the Direct Conversion of Methane to Methanol.Molecules (Basel, Switzerland) · 2022Review
- Structure and activity of particulate methane monooxygenase arrays in methanotrophs.Nature communications · 2022Article
- Microbial oxidation of atmospheric trace gases.Nature reviews. Microbiology · 2022Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Previous biochemical and structural studies of pMMO have focused on preparations from Methylococcus capsulatus (Bath) and Methylosinus trichosporium OB3b. A pMMO from a third organism, Methylocystis species strain M, has been isolated and characterized. Both membrane-bound and solubilized Methylocystis sp. strain M pMMO contain ~2 copper ions per 100 kDa protomer and exhibit copper-dependent propylene epoxidation activity. Spectroscopic data indicate that Methylocystis sp. strain M pMMO contains a mixture of Cu(I) and Cu(II), of which the latter exhibits two distinct type 2 Cu(II) electron paramagnetic resonance (EPR) signals. Extended X-ray absorption fine structure (EXAFS) data are best fit with a mixture of Cu-O/N and Cu-Cu ligand environments with a Cu-Cu interaction at 2.52-2.64 Å. The crystal structure of Methylocystis sp. strain M pMMO was determined to 2.68 Å resolution and is the best quality pMMO structure obtained to date. It provides a revised model for the pmoA and pmoC subunits and has led to an improved model of M. capsulatus (Bath) pMMO. In these new structures, the intramembrane zinc/copper binding site has a different coordination environment from that in previous models.
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