Evidence map›Paper›PMID 26984926›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2016

Methanobactin and the Link between Copper and Bacterial Methane Oxidation.

Alan A DiSpirito, Jeremy D Semrau, J Colin Murrell, Warren H Gallagher, Christopher Dennison, Stéphane Vuilleumier

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
9.7field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

55 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
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  4. Review
  5. Fatuamide A, a Hybrid PKS/NRPS Metallophore from aJournal of natural products · 2025
    Article
  6. A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Review
  8. Article
  9. Article
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  11. Review
  12. Article
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  14. Article
  15. Crystal structure of MbnF: an NADPH-dependent flavin monooxygenase from Methylocystis strain SB2.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  16. Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 6 institutions in 3 countries.

Alan A DiSpiritoRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa, USA aland@iastate.edu.
Jeremy D SemrauDepartment of Civil and Environmental Engineering, University of Michigan, Ann Arbor, Michigan, USA.
J Colin MurrellEarth and Life Systems Alliance, School of Environmental Sciences, University of East Anglia, Norwich, United Kingdom.
Warren H GallagherDepartment of Chemistry, University of Wisconsin-Eau Claire, Eau Claire, Wisconsin, USA.
Christopher DennisonInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne, United Kingdom.
Stéphane VuilleumierDepartment of Microbiology, Genomics and the Environment, UMR 7156 UNISTRA-CNRS, Université de Strasbourg, Strasbourg, France.
Iowa State University · USNewcastle University · GBUniversité de Strasbourg · FRUniversity of East Anglia · GBUniversity of Michigan–Ann Arbor · USUniversity of Wisconsin–Eau Claire · US

Funding

Biotechnology and Biological Sciences Research Council BB/K008439/1
6 · The paper itself

Abstract

Methanobactins (mbs) are low-molecular-mass (<1,200 Da) copper-binding peptides, or chalkophores, produced by many methane-oxidizing bacteria (methanotrophs). These molecules exhibit similarities to certain iron-binding siderophores but are expressed and secreted in response to copper limitation. Structurally, mbs are characterized by a pair of heterocyclic rings with associated thioamide groups that form the copper coordination site. One of the rings is always an oxazolone and the second ring an oxazolone, an imidazolone, or a pyrazinedione moiety. The mb molecule originates from a peptide precursor that undergoes a series of posttranslational modifications, including (i) ring formation, (ii) cleavage of a leader peptide sequence, and (iii) in some cases, addition of a sulfate group. Functionally, mbs represent the extracellular component of a copper acquisition system. Consistent with this role in copper acquisition, mbs have a high affinity for copper ions. Following binding, mbs rapidly reduce Cu(2+) to Cu(1+). In addition to binding copper, mbs will bind most transition metals and near-transition metals and protect the host methanotroph as well as other bacteria from toxic metals. Several other physiological functions have been assigned to mbs, based primarily on their redox and metal-binding properties. In this review, we examine the current state of knowledge of this novel type of metal-binding peptide. We also explore its potential applications, how mbs may alter the bioavailability of multiple metals, and the many roles mbs may play in the physiology of methanotrophs.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesBiodegradation, EnvironmentalCoordination ComplexesCopperGene ExpressionGene Expression Regulation, BacterialImidazolesMetabolic Networks and PathwaysMethaneMethylococcaceaeOligopeptidesOxidation-ReductionProtein BindingSoil PollutantsBacterial ProteinsCoordination ComplexesCopperImidazolesMethanemethanobactinOligopeptidesSoil Pollutants

Identifiers

PMID26984926
PMCPMC4867365
OpenAlexW2301975229

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.