Evidence map›Paper›PMID 20937896›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Initiation of the proton pump of cytochrome c oxidase.

Ilya Belevich, Elena Gorbikova, Nikolai P Belevich, Virve Rauhamäki, Mårten Wikström, Michael I Verkhovsky

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Special Issue "Ion Pumps: Molecular Mechanisms, Structure, Physiology".International journal of molecular sciences · 2026
    Article
  2. Article
  3. Cell Phone Radiation Exposure Limits and Engineering Solutions.International journal of environmental research and public health · 2023
    Review
  4. Review
  5. Review
  6. Probing the Proton-Loading Site of CytochromeMolecules (Basel, Switzerland) · 2020
    Article
  7. Review
  8. Analyzing the electrogenicity of cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Multiscale simulations reveal key features of the proton-pumping mechanism in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Characterizing the proton loading site in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Review
  14. Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Article
  16. 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.

Ilya BelevichHelsinki Bioenergetics Group, Institute of Biotechnology, University of Helsinki, PB 65 (Viikinkaari 1), FI-00014, Helsinki, Finland.
Elena Gorbikova
Nikolai P Belevich
Virve Rauhamäki
Mårten Wikström
Michael I Verkhovsky

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome c oxidase is the terminal enzyme of the respiratory chain that is responsible for biological energy conversion in mitochondria and aerobic bacteria. The membrane-bound enzyme converts free energy from oxygen reduction to an electrochemical proton gradient by functioning as a redox-coupled proton pump. Although the 3D structure and functional studies have revealed proton conducting pathways in the enzyme interior, the location of proton donor and acceptor groups are not fully identified. We show here by time-resolved optical and FTIR spectroscopy combined with time-resolved electrometry that some mutant enzymes incapable of proton pumping nevertheless initiate catalysis by proton transfer to a proton-loading site. A conserved tyrosine in the so-called D-channel is identified as a potential proton donor that determines the efficiency of this reaction.

Indexed as

Amino Acid SubstitutionBacterial ProteinsBiophysical PhenomenaElectrochemistryElectron Transport Complex IVKineticsMembrane PotentialsModels, MolecularMutagenesis, Site-DirectedMutant ProteinsParacoccus denitrificansSpectrophotometrySpectroscopy, Fourier Transform InfraredBacterial ProteinsElectron Transport Complex IVMutant Proteins

Identifiers

PMID20937896
PMCPMC2972982

What OpenQuestion holds

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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.