Evidence map›Paper›PMID 16756489›Full record

ReviewAnnual review of biochemistry2006

Energy transduction: proton transfer through the respiratory complexes.

Jonathan P Hosler, Shelagh Ferguson-Miller, Denise A Mills

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing 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

111 citing papers in PubMed.

  1. Article
  2. Circadian coupling of mitochondria in a deep-diving mammal.The Journal of experimental biology · 2024
    Article
  3. Article
  4. Article
  5. Structural basis of mammalian complex IV inhibition by steroids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Double Proton Transfer Across a Table: The Formic Acid Dimer-Fluorobenzene Complex.Angewandte Chemie (International ed. in English) · 2021
    Article
  8. Article
  9. Review
  10. Biomedical Implants with Charge-Transfer Monitoring and Regulating Abilities.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
    Review
  11. Article
  12. A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Cytochrome aaBiochemistry · 2018
    Article
  20. Voltage and pH sensing by the voltage-gated proton channel, HJournal of the Royal Society, Interface · 2018
    Review

51 more citing papers are in PubMed but not listed here.

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.

Jonathan P HoslerDepartment of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, USA. jhosler@biochem.umsmed.edu
Shelagh Ferguson-Miller
Denise A Mills

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 GM 26916NIGMS NIH HHS GM 56802NIGMS NIH HHS R01 GM026916NIGMS NIH HHS R37 GM026916
6 · The paper itself

Abstract

A series of metalloprotein complexes embedded in a mitochondrial or bacterial membrane utilize electron transfer reactions to pump protons across the membrane and create an electrochemical potential (DeltamuH+). Current understanding of the principles of electron-driven proton transfer is discussed, mainly with respect to the wealth of knowledge available from studies of cytochrome c oxidase. Structural, experimental, and theoretical evidence supports the model of long-distance proton transfer via hydrogen-bonded water chains in proteins as well as the basic concept that proton uptake and release in a redox-driven pump are driven by charge changes at the membrane-embedded centers. Key elements in the pumping mechanism may include bound water, carboxylates, and the heme propionates, arginines, and associated water above the hemes. There is evidence for an important role of subunit III and proton backflow, but the number and nature of gating mechanisms remain elusive, as does the mechanism of physiological control of efficiency.

Indexed as

Electron Transport Complex IVOxidative PhosphorylationProtonsBinding SitesElectron TransportElectron Transport Chain Complex ProteinsEnergy MetabolismHemeOxidation-ReductionProtein ConformationProtein SubunitsStatic ElectricityThermodynamicsWaterElectron Transport Chain Complex ProteinsElectron Transport Complex IVHemeProtein SubunitsProtonsWater

Identifiers

PMID16756489
PMCPMC2659341

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.