ArticleProceedings of the National Academy of Sciences of the United States of America2016
Methanobactin transport machinery.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 63 citations in OpenAlex.
- From antibiotic to chalkophore: the biology and evolution of SF2768 in Streptomyces.Essays in biochemistry · 2026Review
- Methane cycling microbes are important predictors of methylmercury accumulation in rice paddies.Applied and environmental microbiology · 2026Article
- A new family of TonB-dependent copper transporters linked to respiratory oxidase function.The Journal of biological chemistry · 2026Article
- Navigating the copper highway: bacterial strategies for cytoplasmic import.Journal of inorganic biochemistry · 2026Review
- CrpH ofFrontiers in microbiology · 2026Article
- The Escherichia coli AZY operon links copper uptake to antibiotic resistance.Communications biology · 2025Article
- Trojan horse peptide conjugates remodel the activity spectrum of clinical antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Methanobactins: Structures, Biosynthesis, and Microbial Diversity.Annual review of microbiology · 2024Review
- A multi-iron enzyme installs copper-binding oxazolone/thioamide pairs on a nontypeableProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.Current opinion in chemical biology · 2024Review
- Molecular basis for substrate transport ofScience advances · 2024Article
- 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
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- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Teaching the chemical elements in biochemistry: Elemental biology and metallomics.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology · 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
- Evidence for methanobactin "Theft" and novel chalkophore production in methanotrophs: impact on methanotrophic-mediated methylmercury degradation.The ISME journal · 2022Article
- Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.PLoS biology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Methanotrophic bacteria use methane, a potent greenhouse gas, as their primary source of carbon and energy. The first step in methane metabolism is its oxidation to methanol. In almost all methanotrophs, this chemically challenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integral membrane enzyme. Methanotrophs acquire copper (Cu) for pMMO by secreting a small ribosomally produced, posttranslationally modified natural product called methanobactin (Mbn). Mbn chelates Cu with high affinity, and the Cu-loaded form (CuMbn) is reinternalized into the cell via an active transport process. Bioinformatic and gene regulation studies suggest that two proteins might play a role in CuMbn handling: the TonB-dependent transporter MbnT and the periplasmic binding protein MbnE. Disruption of the gene that encodes MbnT abolishes CuMbn uptake, as reported previously, and expression of MbnT in Escherichia coli confers the ability to take up CuMbn. Biophysical studies of MbnT and MbnE reveal specific interactions with CuMbn, and a crystal structure of apo MbnE is consistent with MbnE's proposed role as a periplasmic CuMbn transporter. Notably, MbnT and MbnE exhibit different levels of discrimination between cognate and noncognate CuMbns. These findings provide evidence for CuMbn-protein interactions and begin to elucidate the molecular mechanisms of its recognition and transport.
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