ArticlePloS one2012
The Methylococcus capsulatus (Bath) secreted protein, MopE*, binds both reduced and oxidized copper.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Complete genome sequences ofMicrobiology resource announcements · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Evidence for methanobactin "Theft" and novel chalkophore production in methanotrophs: impact on methanotrophic-mediated methylmercury degradation.The ISME journal · 2022Article
- Copper binding by a unique family of metalloproteins is dependent on kynurenine formation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- From nature to nurture: Essence and methods to isolate robust methanotrophic bacteria.Synthetic and systems biotechnology · 2020Article
- MbnH is a diheme MauG-like protein associated with microbial copper homeostasis.The Journal of biological chemistry · 2019Article
- Aerobic methane oxidation under copper scarcity in a stratified lake.Scientific reports · 2019Article
- Efficient Counterselection for Methylococcus capsulatus (Bath) by Using a MutatedApplied and environmental microbiology · 2018Article
- Chalkophores.Annual review of biochemistry · 2018Review
- Metals and Methanotrophy.Applied and environmental microbiology · 2018Review
- Anaerobic Copper Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli.Applied and environmental microbiology · 2017Article
- Methanobactins: from genome to function.Metallomics : integrated biometal science · 2017Review
- Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases.MicrobiologyOpen · 2016Article
- A TonB-Dependent Transporter Is Responsible for Methanobactin Uptake by Methylosinus trichosporium OB3b.Applied and environmental microbiology · 2016Article
- Methanobactin from Methylocystis sp. strain SB2 affects gene expression and methane monooxygenase activity in Methylosinus trichosporium OB3b.Applied and environmental microbiology · 2015Article
- Copper binding in IscA inhibits iron-sulphur cluster assembly in Escherichia coli.Molecular microbiology · 2014Article
- CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.PloS one · 2014Article
- Detoxification of mercury by methanobactin from Methylosinus trichosporium OB3b.Applied and environmental microbiology · 2013Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Under copper limiting growth conditions the methanotrophic bacterium Methylococcus capsulatus (Bath) secrets essentially only one protein, MopE*, to the medium. MopE* is a copper-binding protein whose structure has been determined by X-ray crystallography. The structure of MopE* revealed a unique high affinity copper binding site consisting of two histidine imidazoles and one kynurenine, the latter an oxidation product of Trp130. In this study, we demonstrate that the copper ion coordinated by this strong binding site is in the Cu(I) state when MopE* is isolated from the growth medium of M. capsulatus. The conclusion is based on X-ray Near Edge Absorption spectroscopy (XANES), and Electron Paramagnetic Resonance (EPR) studies. EPR analyses demonstrated that MopE*, in addition to the strong copper-binding site, also binds Cu(II) at two weaker binding sites. Both Cu(II) binding sites have properties typical of non-blue type II Cu (II) centres, and the strongest of the two Cu(II) sites is characterised by a relative high hyperfine coupling of copper (A(||) =20 mT). Immobilized metal affinity chromatography binding studies suggests that residues in the N-terminal part of MopE* are involved in forming binding site(s) for Cu(II) ions. Our results support the hypothesis that MopE plays an important role in copper uptake, possibly making use of both its high (Cu(I) and low Cu(II) affinity properties.
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