Evidence map›Paper›PMID 23799249›Full record

ArticleJournal of the American Chemical Society2013

Protein-protein interaction regulates the direction of catalysis and electron transfer in a redox enzyme complex.

Duncan G G McMillan, Sophie J Marritt, Mackenzie A Firer-Sherwood, Liang Shi, David J Richardson, Stephen D Evans, Sean J Elliott, Julea N Butt, Lars J C Jeuken

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review
  3. Article
  4. Decoding in-cell respiratory enzyme dynamics by label-free in situ electrochemistry.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. A nondestructive membrane engineering method using an amphiphilic polymer.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Promoting Extracellular Electron Transfer ofFrontiers in microbiology · 2021
    Article
  18. Interaction of Silver-Lignin Nanoparticles With Mammalian Mimetic Membranes.Frontiers in bioengineering and biotechnology · 2020
    Article
  19. Article
  20. 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

9 authors at 5 institutions in 3 countries.

Duncan G G McMillanSchool of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom.
Sophie J Marritt
Mackenzie A Firer-Sherwood
Liang Shi
David J Richardson
Stephen D Evans
Sean J Elliott
Julea N Butt
Lars J C Jeuken
Boston University · USUniversity of East Anglia · GBUniversity of Leeds · GBBattelle · USCentre for Structural Systems Biology · DE

Funding

Biotechnology and Biological Sciences Research Council BB/G007519/1Biotechnology and Biological Sciences Research Council BB/G009228Biotechnology and Biological Sciences Research Council BB/G009228/1
6 · The paper itself

Abstract

Protein-protein interactions are well-known to regulate enzyme activity in cell signaling and metabolism. Here, we show that protein-protein interactions regulate the activity of a respiratory-chain enzyme, CymA, by changing the direction or bias of catalysis. CymA, a member of the widespread NapC/NirT superfamily, is a menaquinol-7 (MQ-7) dehydrogenase that donates electrons to several distinct terminal reductases in the versatile respiratory network of Shewanella oneidensis . We report the incorporation of CymA within solid-supported membranes that mimic the inner membrane architecture of S. oneidensis . Quartz-crystal microbalance with dissipation (QCM-D) resolved the formation of a stable complex between CymA and one of its native redox partners, flavocytochrome c3 (Fcc3) fumarate reductase. Cyclic voltammetry revealed that CymA alone could only reduce MQ-7, while the CymA-Fcc3 complex catalyzed the reaction required to support anaerobic respiration, the oxidation of MQ-7. We propose that MQ-7 oxidation in CymA is limited by electron transfer to the hemes and that complex formation with Fcc3 facilitates the electron-transfer rate along the heme redox chain. These results reveal a yet unexplored mechanism by which bacteria can regulate multibranched respiratory networks through protein-protein interactions.

Indexed as

BiocatalysisCytochrome c GroupElectron TransportModels, MolecularOxidation-ReductionProtein BindingShewanellacytochrome c(3)Cytochrome c Group

Identifiers

PMID23799249
PMCPMC3823026
OpenAlexW1979540793

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.