ArticleThe Journal of biological chemistry2014
Effects of zinc on particulate methane monooxygenase activity and structure.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 85 citations in OpenAlex.
- Membrane properties modulate methane oxidation by particulate methane monooxygenase.The Journal of biological chemistry · 2026Article
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- When the wrong metal stops the cycle: Dynamics and specificity in plant copper-dependent peptide cyclases.Journal of inorganic biochemistry · 2026Article
- Assessment and functional genomic investigation of methane and nitrogen metabolizing pathways in Pseudomonas aeruginosa strain AAK/M5.World journal of microbiology & biotechnology · 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
- Microbial Responses to Micronutrient Amendments in Oxygenated and Deoxygenated Waters of the Arabian Sea.Environmental microbiology reports · 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
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Product analog binding identifies the copper active site of particulate methane monooxygenase.Nature catalysis · 2023Article
- Methane Oxidation to Methanol.Chemical reviews · 2023Review
- 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
- Structure and activity of particulate methane monooxygenase arrays in methanotrophs.Nature communications · 2022Article
- Microbial oxidation of atmospheric trace gases.Nature reviews. Microbiology · 2022Review
- Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer.Science (New York, N.Y.) · 2022Article
- Sustainable biosynthesis of chemicals from methane and glycerol via reconstruction of multi-carbon utilizing pathway in obligate methanotrophic bacteria.Microbial biotechnology · 2021Article
- Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the CuJournal of the American Chemical Society · 2021Article
- C-H Bond Cleavage by Bioinspired Nonheme Metal Complexes.Inorganic chemistry · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Particulate methane monooxygenase (pMMO) is a membrane-bound metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Zinc is a known inhibitor of pMMO, but the details of zinc binding and the mechanism of inhibition are not understood. Metal binding and activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibits pMMO at two sites that are distinct from the copper active site. The 2.6 Å resolution crystal structure of Methylocystis species strain Rockwell pMMO reveals two previously undetected bound lipids, and metal soaking experiments identify likely locations for the two zinc inhibition sites. The first is the crystallographic zinc site in the pmoC subunit, and zinc binding here leads to the ordering of 10 previously unobserved residues. A second zinc site is present on the cytoplasmic side of the pmoC subunit. Parallels between these results and zinc inhibition studies of several respiratory complexes suggest that zinc might inhibit proton transfer in pMMO.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.