ArticleProceedings of the National Academy of Sciences of the United States of America2012
Variations in methanobactin structure influences copper utilization by methane-oxidizing bacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 88 citations in OpenAlex.
- Copper homeostasis networks in pseudomonas aeruginosa and the organocopper metabolite fluopsin C.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Review
- Regulatory mechanisms of CHFrontiers in microbiology · 2026Article
- Methanobactins: Structures, Biosynthesis, and Microbial Diversity.Annual review of microbiology · 2024Review
- Genome mining of sulfonated lanthipeptides reveals unique cyclic peptide sulfotransferases.Acta pharmaceutica Sinica. B · 2024Article
- Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.Current opinion in chemical biology · 2024Review
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Purification and biochemical characterization of methanobactin biosynthetic enzymes.Methods in enzymology · 2024Article
- Crystal structure of MbnF: an NADPH-dependent flavin monooxygenase from Methylocystis strain SB2.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Ecological Aerobic Ammonia and Methane Oxidation Involved Key Metal Compounds, Fe and Cu.Life (Basel, Switzerland) · 2022Review
- Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Variable Inhibition of Nitrous Oxide Reduction in Denitrifying Bacteria by Different Forms of Methanobactin.Applied and environmental microbiology · 2022Article
- A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Crystal structure and catalytic mechanism of the MbnBC holoenzyme required for methanobactin biosynthesis.Cell research · 2022Article
- MbnC Is Not Required for the Formation of the N-Terminal Oxazolone in the Methanobactin from Methylosinus trichosporium OB3b.Applied and environmental microbiology · 2022Article
- Two TonB-Dependent Transporters in Methylosinus trichosporium OB3b Are Responsible for Uptake of Different Forms of Methanobactin and Are Involved in the Canonical "Copper Switch".Applied and environmental microbiology · 2022Article
- Characterization of a Copper-Chelating Natural Product from the MethanotrophBiochemistry · 2021Article
- Metal(loid) speciation and transformation by aerobic methanotrophs.Microbiome · 2021Review
- Oxygen Generation via Water Splitting by a Novel Biogenic Metal Ion-Binding Compound.Applied and environmental microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methane-oxidizing bacteria are nature's primary biological mechanism for suppressing atmospheric levels of the second-most important greenhouse gas via methane monooxygenases (MMOs). The copper-containing particulate enzyme is the most widespread and efficient MMO. Under low-copper conditions methane-oxidizing bacteria secrete the small copper-binding peptide methanobactin (mbtin) to acquire copper, but how variations in the structures of mbtins influence copper metabolism and species selection are unknown. Methanobactins have been isolated from Methylocystis strains M and hirsuta CSC1, organisms that can switch to using an iron-containing soluble MMO when copper is limiting, and the nonswitchover Methylocystis rosea. These mbtins are shorter, and have different amino acid compositions, than the characterized mbtin from Methylosinus trichosporium OB3b. A coordinating pyrazinedione ring in the Methylocystis mbtins has little influence on the Cu(I) site structure. The Methylocystis mbtins have a sulfate group that helps stabilize the Cu(I) forms, resulting in affinities of approximately 10(21) M(-1). The Cu(II) affinities vary over three orders of magnitude with reduction potentials covering approximately 250 mV, which may dictate the mechanism of intracellular copper release. Copper uptake and the switchover from using the iron-containing soluble MMO to the copper-containing particulate enzyme is faster when mediated by the native mbtin, suggesting that the amino acid sequence is important for the interaction of mbtins with receptors. The differences in structures and properties of mbtins, and their influence on copper utilization by methane-oxidizing bacteria, have important implications for the ecology and global function of these environmentally vital organisms.
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