Evidence map›Paper›PMID 18830692›Full record

ArticleJournal of bioenergetics and biomembranes2008

A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases.

Martyn A Sharpe, Shelagh Ferguson-Miller

Open access · greenAbstract read
In one paragraph

Article in Journal of bioenergetics and biomembranes, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 72 citations in OpenAlex.

  1. Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Mutation of a single residue in the ba3 oxidase specifically impairs protonation of the pump site.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Review
  10. Characterizing the proton loading site in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Review
  12. Copper active sites in biology.Chemical reviews · 2014
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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
  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 1 country.

Martyn A SharpeDepartment of Neurosurgery, The Methodist Hospital, Houston, TX 77030, USA. MASharpe@tmhs.org
Shelagh Ferguson-Miller
Methodist Hospital · USMichigan State University · US

Funding

ENERGY TRANSDUCTION IN CYTOCHROME OXIDASER37GM026916 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FERGUSON-MILLER, SHELAGH M · 2000 to 2010
$3.5M
ORGANIZATION AND CONTROL OF ELECTRON TRANSFER CHAINSR01GM026916 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FERGUSON-MILLER, SHELAGH M · 1985 to 2014
$1.6M
NIGMS NIH HHS R01 GM026916NIGMS NIH HHS R37 GM026916
6 · The paper itself

Abstract

A mechanism for proton pumping is described that is based on chemiosmotic principles and the detailed molecular structures now available for cytochrome oxidases. The importance of conserved water positions and a step-wise gated process of proton translocation is emphasized, where discrete electron transfer events are coupled to proton uptake and expulsion. The trajectory of each pumped proton is the same for all four substrate electrons. An essential role for the His-Tyr cross-linked species is discussed, in gating of the D- and K-channels and as an acceptor/donor of electrons and protons at the binuclear center.

Indexed as

CopperElectron Transport Complex IVHemeIon Channel GatingMagnesiumModels, BiologicalModels, MolecularOxidation-ReductionPotassium ChannelsProton-Motive ForceProton PumpsStatic ElectricityWaterCopperElectron Transport Complex IVHemeMagnesiumPotassium ChannelsProton PumpsWater

Identifiers

PMID18830692
PMCPMC2613019
OpenAlexW2037970486

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.