Evidence map›Paper›PMID 22392981›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications.

Mårten Wikström, Gerhard Hummer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Architecture of bacterial respiratory chains.Nature reviews. Microbiology · 2021
    Review
  12. Article
  13. Article
  14. Energy-converting hydrogenases: the link between HCellular and molecular life sciences : CMLS · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. Redox-coupled quinone dynamics in the respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  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 2 institutions in 2 countries.

Mårten WikströmHelsinki Bioenergetics Group, Institute of Biotechnology, University of Helsinki, FI-00014 Helsinki, Finland.
Gerhard Hummer
National Institute of Diabetes and Digestive and Kidney Diseases · USUniversity of Helsinki · FI

Funding

Theory and simulation of protein dynamics, folding, and functionZIADK029033 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2009 to 2013
$3.3M
Water, protons, and ions biomolecular systemsZIADK029036 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2009 to 2012
$1.9M
Intramural NIH HHS
6 · The paper itself

Abstract

Complex I (NADH-ubiquinone oxidoreductase) in the respiratory chain of mitochondria and several bacteria functions as a redox-driven proton pump that contributes to the generation of the protonmotive force across the inner mitochondrial or bacterial membrane and thus to the aerobic synthesis of ATP. The stoichiometry of proton translocation is thought to be 4 H(+) per NADH oxidized (2 e(-)). Here we show that a H(+)/2 e(-) ratio of 3 appears more likely on the basis of the recently determined H(+)/ATP ratio of the mitochondrial F(1)F(o)-ATP synthase of animal mitochondria and of a set of carefully determined ATP/2 e(-) ratios for different segments of the mitochondrial respiratory chain. This lower H(+)/2 e(-) ratio of 3 is independently supported by thermodynamic analyses of experiments with both mitochondria and submitochondrial particles. A reduced H(+)/2 e(-) stoichiometry of 3 has important mechanistic implications for this proton pump. In a rough mechanistic model, we suggest a concerted proton translocation mechanism in the three homologous and tightly packed antiporter-like subunits L, M, and N of the proton-translocating membrane domain of complex I.

Indexed as

Adenosine TriphosphateBinding SitesBiological TransportCell MembraneCell RespirationElectron Transport Complex IEscherichia coliMitochondriaOxidation-ReductionOxidative PhosphorylationPhosphorylationProtein ConformationProton-Motive ForceProtonsProton-Translocating ATPasesThermodynamicsAdenosine TriphosphateElectron Transport Complex IProtonsProton-Translocating ATPases

Identifiers

PMID22392981
PMCPMC3311377
OpenAlexW2022259714

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.