Evidence map›Paper›PMID 21454533›Full record

ArticleThe Journal of biological chemistry2011

A model of the proton translocation mechanism of complex I.

Jason R Treberg, Martin D Brand

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Modelling mitochondrial ROS production by the respiratory chain.Cellular and molecular life sciences : CMLS · 2020
    Review
  6. Redox-coupled quinone dynamics in the respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Review
  8. Article
  9. Review
  10. Symmetry-related proton transfer pathways in respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
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

2 authors at 1 institution in 1 country.

Jason R TrebergBuck Institute for Research on Aging, Novato, California 94945, USA. jtreberg@mun.ca
Martin D Brand
Buck Institute for Research on Aging · US

Funding

PROTEOMICSP01AG025901 · NIA · BUCK INSTITUTE FOR RESEARCH ON AGING · PI GIBSON, BRADFORD WAYNE · 2007 to 2011
$8.6M
Mass spectrometry and imaging technologies in GerosciencePL1AG032118 · NIA · BUCK INSTITUTE FOR RESEARCH ON AGING · PI GIBSON, BRADFORD WAYNE · 2007 to 2011
$4.5M
Mitochondrial sites of reactive oxygen species generation in cells.R01AG033542 · NIA · BUCK INSTITUTE FOR RESEARCH ON AGING · PI BRAND, MARTIN D · 2009 to 2010
$970k
NIA NIH HHS P01 AG025901NIA NIH HHS PL1 AG032118NIA NIH HHS R01 AG033542
6 · The paper itself

Abstract

Despite decades of speculation, the proton pumping mechanism of complex I (NADH-ubiquinone oxidoreductase) is unknown and continues to be controversial. Recent descriptions of the architecture of the hydrophobic region of complex I have resolved one vital issue: this region appears to have multiple proton transporters that are mechanically interlinked. Thus, transduction of conformational changes to drive the transmembrane transporters linked by a "connecting rod" during the reduction of ubiquinone (Q) can account for two or three of the four protons pumped per NADH oxidized. The remaining proton(s) must be pumped by direct coupling at the Q-binding site. Here, we present a mixed model based on a crucial constraint: the strong dependence on the pH gradient across the membrane (ΔpH) of superoxide generation at the Q-binding site of complex I. This model combines direct and indirect coupling mechanisms to account for the pumping of the four protons. It explains the observed properties of the semiquinone in the Q-binding site, the rapid superoxide production from this site during reverse electron transport, its low superoxide production during forward electron transport except in the presence of inhibitory Q-analogs and high protonmotive force, and the strong dependence of both modes of superoxide production on ΔpH.

Indexed as

Models, ChemicalProtonsElectron Transport Complex IEscherichia coliEscherichia coli ProteinsNADOxidation-ReductionThermus thermophilusUbiquinoneElectron Transport Complex IEscherichia coli ProteinsNADProtonsUbiquinone

Identifiers

PMID21454533
PMCPMC3093832
OpenAlexW2087970720

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.