Evidence map›Paper›PMID 20599678›Full record

ArticleBiochimica et biophysica acta2010

Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I).

S Tsuyoshi Ohnishi, John C Salerno, Tomoko Ohnishi

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Redox-induced activation of the proton pump in the respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  5. On the mechanism of respiratory complex I.Journal of bioenergetics and biomembranes · 2014
    Review
  6. Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Article
  8. Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  9. Article
  10. Article
  11. A model of the proton translocation mechanism of complex I.The Journal of biological chemistry · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. 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

3 authors at 2 institutions in 1 country.

S Tsuyoshi OhnishiJohnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
John C Salerno
Tomoko Ohnishi
Johnson Foundation · USKennesaw State University · US

Funding

PROTON &ELECTRON TRANSFER &ENERGY COUPLING IN SIT IR01GM030736 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OHNISHI, TOMOKO NONE · 1985 to 2010
$3.1M
NIGMS NIH HHS R01 GM030736NIGMS NIH HHS R01GM030736
6 · The paper itself

Abstract

In many energy transducing systems which couple electron and proton transport, for example, bacterial photosynthetic reaction center, cytochrome bc(1)-complex (complex III) and E. coli quinol oxidase (cytochrome bo(3) complex), two protein-associated quinone molecules are known to work together. T. Ohnishi and her collaborators reported that two distinct semiquinone species also play important roles in NADH-ubiquinone oxidoreductase (complex I). They were called SQ(Nf) (fast relaxing semiquinone) and SQ(Ns) (slow relaxing semiquinone). It was proposed that Q(Nf) serves as a "direct" proton carrier in the semiquinone-gated proton pump (Ohnishi and Salerno, FEBS Letters 579 (2005) 4555), while Q(Ns) works as a converter between one-electron and two-electron transport processes. This communication presents a revised hypothesis in which Q(Nf) plays a role in a "direct" redox-driven proton pump, while Q(Ns) triggers an "indirect" conformation-driven proton pump. Q(Nf) and Q(Ns) together serve as (1e(-)/2e(-)) converter, for the transfer of reducing equivalent to the Q-pool.

Indexed as

AnimalsBenzoquinonesBiological TransportCattleCell MembraneElectron TransportElectron Transport Complex IHydrogen-Ion ConcentrationModels, BiologicalMyocardiumNADOxidation-ReductionProton PumpsProtonsBenzoquinonesElectron Transport Complex INADProton PumpsProtonsquinone

Identifiers

PMID20599678
PMCPMC2997716
OpenAlexW2032101013

What OpenQuestion holds

Textmetadata
LicenceTDM
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.