Evidence map›Paper›PMID 25012073›Full record

ArticleScientific reports2014

Cell-secreted flavins bound to membrane cytochromes dictate electron transfer reactions to surfaces with diverse charge and pH.

Akihiro Okamoto, Shafeer Kalathil, Xiao Deng, Kazuhito Hashimoto, Ryuhei Nakamura, Kenneth H Nealson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
11.7field-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

41 citing papers in PubMed, 173 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
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  14. Thermodynamic controls on rates of iron oxide reduction by extracellular electron shuttles.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  19. Review
  20. Multifaceted aspects of charge transfer.Physical chemistry chemical physics : PCCP · 2020
    Article
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 4 institutions in 2 countries.

Akihiro Okamoto1] Departments of Earth Sciences and Biological Sciences, University of Southern California, Los Angeles, CA 90089 [2] Department of Applied Chemistry, University of Tokyo, Bunkyo-ku, Tokyo, 113-8654.
Shafeer KalathilDepartment of Applied Chemistry, University of Tokyo, Bunkyo-ku, Tokyo, 113-8654.
Xiao DengDepartment of Applied Chemistry, University of Tokyo, Bunkyo-ku, Tokyo, 113-8654.
Kazuhito HashimotoDepartment of Applied Chemistry, University of Tokyo, Bunkyo-ku, Tokyo, 113-8654.
Ryuhei NakamuraBiofunctional Catalyst Research Team, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Kenneth H Nealson1] Departments of Earth Sciences and Biological Sciences, University of Southern California, Los Angeles, CA 90089 [2] J. Craig Venter Institute, San Diego, CA 92121.
The University of Tokyo · JPJ. Craig Venter Institute · USRIKEN Center for Sustainable Resource Science · JPUniversity of Southern California · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The variety of solid surfaces to and from which microbes can deliver electrons by extracellular electron transport (EET) processes via outer-membrane c-type cytochromes (OM c-Cyts) expands the importance of microbial respiration in natural environments and industrial applications. Here, we demonstrate that the bifurcated EET pathway of OM c-Cyts sustains the diversity of the EET surface in Shewanella oneidensis MR-1 via specific binding with cell-secreted flavin mononucleotide (FMN) and riboflavin (RF). Microbial current production and whole-cell differential pulse voltammetry revealed that RF and FMN enhance EET as bound cofactors in a similar manner. Conversely, FMN and RF were clearly differentiated in the EET enhancement by gene-deletion of OM c-Cyts and the dependency of the electrode potential and pH. These results indicate that RF and FMN have specific binding sites in OM c-Cyts and highlight the potential roles of these flavin-cytochrome complexes in controlling the rate of electron transfer to surfaces with diverse potential and pH.

Indexed as

Binding SitesCytochrome c GroupElectronsElectron TransportFlavin MononucleotideFlavinsHydrogen-Ion ConcentrationMembranesRiboflavinShewanellaCytochrome c GroupFlavin MononucleotideFlavinsRiboflavin

Identifiers

PMID25012073
PMCPMC4092373
OpenAlexW2041547233

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.