Evidence map›Paper›PMID 17675441›Full record

ArticleApplied and environmental microbiology2007

Characterization of protein-protein interactions involved in iron reduction by Shewanella oneidensis MR-1.

Daniel E Ross, Shane S Ruebush, Susan L Brantley, Robert S Hartshorne, Thomas A Clarke, David J Richardson, Ming Tien

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
10.7field-weighted citation impact, top 1% 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

71 citing papers in PubMed, 164 citations in OpenAlex.

  1. Article
  2. Multi-technique characterization of iron reduction by an AntarcticApplied and environmental microbiology · 2025
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  6. Review
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  8. Lack of Specificity inJournal of bacteriology · 2022
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  9. Single molecule tracking of bacterial cell surface cytochromes reveals dynamics that impact long-distance electron transport.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Tuning Extracellular Electron Transfer byACS synthetic biology · 2020
    Article
  15. Article
  16. Biological synthesis of iron nanoparticles using hydrolysates from a waste-based biorefinery.Environmental science and pollution research international · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Daniel E RossDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Shane S Ruebush
Susan L Brantley
Robert S Hartshorne
Thomas A Clarke
David J Richardson
Ming Tien
University of East Anglia · GBPennsylvania State University · US

Funding

Biotechnology and Biological Sciences Research Council B18695
6 · The paper itself

Abstract

The interaction of proteins implicated in dissimilatory metal reduction by Shewanella oneidensis MR-1 (outer membrane [OM] proteins OmcA, MtrB, and MtrC; OM-associated protein MtrA; periplasmic protein CctA; and cytoplasmic membrane protein CymA) were characterized by protein purification, analytical ultracentrifugation, and cross-linking methods. Five of these proteins are heme proteins, OmcA (83 kDa), MtrC (75 kDa), MtrA (32 kDa), CctA (19 kDa), and CymA (21 kDa), and can be visualized after sodium dodecyl sulfate-polyacrylamide gel electrophoresis by heme staining. We show for the first time that MtrC, MtrA, and MtrB form a 198-kDa complex with a 1:1:1 stoichiometry. These proteins copurify through anion-exchange chromatography, and the purified complex has the ability to reduce multiple forms of Fe(III) and Mn(IV). Additionally, MtrA fractionates with the OM through sucrose density gradient ultracentrifugation, and MtrA comigrates with MtrB in native gels. Protein cross-linking of whole cells with 1% formaldehyde show new heme bands of 160, 151, 136, and 59 kDa. Using antibodies to detect each protein separately, heme proteins OmcA and MtrC were shown to cross-link, yielding the 160-kDa band. Consistent with copurification results, MtrB cross-links with MtrA, forming high-molecular-mass bands of approximately 151 and 136 kDa.

Indexed as

Bacterial Outer Membrane ProteinsCytochrome c GroupFerric CompoundsHemeMultigene FamilyOxidation-ReductionProtein BindingProtein Interaction MappingShewanellaBacterial Outer Membrane ProteinsCytochrome c GroupFerric CompoundsHemeMtrC protein, Shewanella

Identifiers

PMID17675441
PMCPMC2074908
OpenAlexW2104794537

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.