Evidence map›Paper›PMID 19366614›Full record

ReviewBiochimica et biophysica acta2009

Architecture of complex I and its implications for electron transfer and proton pumping.

Volker Zickermann, Stefan Kerscher, Klaus Zwicker, Maja A Tocilescu, Michael Radermacher, Ulrich Brandt

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Aging ofCells · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Diet induced the change of mtDNA copy number and metabolism in Angus cattle.Journal of animal science and biotechnology · 2020
    Article
  10. Mutations inCells · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Upstream Pathways Controlling Mitochondrial Function in Major Psychosis: A Focus on Bipolar Disorder.Canadian journal of psychiatry. Revue canadienne de psychiatrie · 2016
    Review
  18. 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

6 authors at 2 institutions in 2 countries.

Volker ZickermannGoethe-Universität, Fachbereich Medizin, Molekulare Bioenergetik, ZBC, Theodor-Stern-Kai 7, Haus 26, D-60590 Frankfurt am Main, Germany.
Stefan Kerscher
Klaus Zwicker
Maja A Tocilescu
Michael Radermacher
Ulrich Brandt
Goethe University Frankfurt · DEUniversity of Vermont · US

Funding

3D Structure of Membrane ProteinsR01GM068650 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI RADERMACHER, MICHAEL · 2003 to 2013
$2.4M
NIGMS NIH HHS R01 GM068650
6 · The paper itself

Abstract

Proton pumping NADH:ubiquinone oxidoreductase (complex I) is the largest and remains by far the least understood enzyme complex of the respiratory chain. It consists of a peripheral arm harbouring all known redox active prosthetic groups and a membrane arm with a yet unknown number of proton translocation sites. The ubiquinone reduction site close to iron-sulfur cluster N2 at the interface of the 49-kDa and PSST subunits has been mapped by extensive site directed mutagenesis. Independent lines of evidence identified electron transfer events during reduction of ubiquinone to be associated with the potential drop that generates the full driving force for proton translocation with a 4H(+)/2e(-) stoichiometry. Electron microscopic analysis of immuno-labelled native enzyme and of a subcomplex lacking the electron input module indicated a distance of 35-60 A of cluster N2 to the membrane surface. Resolution of the membrane arm into subcomplexes showed that even the distal part harbours subunits that are prime candidates to participate in proton translocation because they are homologous to sodium/proton antiporters and contain conserved charged residues in predicted transmembrane helices. The mechanism of redox linked proton translocation by complex I is largely unknown but has to include steps where energy is transmitted over extremely long distances. In this review we compile the available structural information on complex I and discuss implications for complex I function.

Indexed as

Catalytic DomainCrystallography, X-RayElectron TransportElectron Transport Complex IFungal ProteinsHydrophobic and Hydrophilic InteractionsImaging, Three-DimensionalModels, MolecularProtein ConformationProtein SubunitsProton PumpsYarrowiaElectron Transport Complex IFungal ProteinsProtein SubunitsProton Pumps

Identifiers

PMID19366614
PMCPMC2699368
OpenAlexW2065229855

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.