Evidence map›Paper›PMID 23201476›Full record

ReviewBiochimica et biophysica acta

Structural analysis of cytochrome bc1 complexes: implications to the mechanism of function.

Di Xia, Lothar Esser, Wai-Kwan Tang, Fei Zhou, Yihui Zhou, Linda Yu, Chang-An Yu

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

90 citing papers in PubMed, 185 citations in OpenAlex.

  1. Review
  2. Distinct ubiquinone binding at the oxidation and reduction sites of cytochrome bcProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Flexibility and Hydration of the QJournal of chemical information and modeling · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Redox-Activated Proton Transfer through a Redundant Network in the QJournal of chemical information and modeling · 2025
    Article
  14. Understanding coenzyme Q.Physiological reviews · 2024
    Review
  15. Dual diagnosis ofRare (Amsterdam, Netherlands) · 2024
    Article
  16. Review
  17. Article
  18. Structure and function of theProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

30 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

7 authors at 2 institutions in 1 country.

Di XiaLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: xiad@mail.nih.gov.
Lothar Esser
Wai-Kwan Tang
Fei Zhou
Yihui Zhou
Linda Yu
Chang-An Yu
National Institutes of Health · USOklahoma State University · US

Funding

Structural Basis of Biological Membrane Protein Functions and Drug ResistanceZIABC010319 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 2009 to 2025
$22.7M
REACTION MECHANISM OF MYOCARDIAC UBIQUINONE-PROTEINSR37GM030721 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI YU, CHANG-AN · 2000 to 2009
$4.6M
Structural Analysis of Biological Membrane Proteins andZ01BC010319 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 1999 to 2008
$1.7M
REACTION MECHANISMS OF MYOCARDIAL UBIQUINONE-PROTEINSR01GM030721 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI YU, CHANG-AN · 1985 to 1999
–
Intramural NIH HHS Z01 BC010319Intramural NIH HHS ZIA BC010319NIGMS NIH HHS GM30721NIGMS NIH HHS R01 GM030721NIGMS NIH HHS R37 GM030721
6 · The paper itself

Abstract

The cytochrome bc1 complex (bc1) is the mid-segment of the cellular respiratory chain of mitochondria and many aerobic prokaryotic organisms; it is also part of the photosynthetic apparatus of non-oxygenic purple bacteria. The bc1 complex catalyzes the reaction of transferring electrons from the low potential substrate ubiquinol to high potential cytochrome c. Concomitantly, bc1 translocates protons across the membrane, contributing to the proton-motive force essential for a variety of cellular activities such as ATP synthesis. Structural investigations of bc1 have been exceedingly successful, yielding atomic resolution structures of bc1 from various organisms and trapped in different reaction intermediates. These structures have confirmed and unified results of decades of experiments and have contributed to our understanding of the mechanism of bc1 functions as well as its inactivation by respiratory inhibitors. This article is part of a Special Issue entitled: Respiratory complex III and related bc complexes.

Indexed as

Protein ConformationElectron TransportElectron Transport Complex IIIMetalsModels, MolecularPhospholipidsProtein BindingProtein SubunitsSubstrate SpecificityElectron Transport Complex IIIMetalsPhospholipidsProtein Subunitsbc(1)bc(1) from Saccharomyces cerevisiaeb(H)Bifurcated electron flowb(L)Bos taurus bc(1)Btbc(1)CAcardiolipinCLcomplex III or ubiquinol cytochrome c oxidoreductase or cytochrome bc(1)contact areaControl of ISP domain movementCrystal structureCytochrome bc(1) complexelectron transferETextrinsic domain of ISPfrom Rhodobacter sphaeroidesGallus gallus bc(1)Ggbc(1)high-potential heme or b(562)iron–sulfur clusteriron–sulfur proteinISCISPISP-EDlow-potential heme or b(566)Mechanism of ubiquinol oxidationmitochondrial bc(1)mitochondrial processing peptidaseMPPMtbc(1)NCSNon-crystallographic symmetryPCPDBPEphosphatidylcholinephosphatidylethanolaminephosphatidylinositolPIprotein data bankQQH(2)Q(N)Q(P)rms deviationroot-mean-square deviationSCScbc(1)surface complementarityTMtransmembraneubiquinolubiquinol oxidation,Rsbc(1)ubiquinoneubiquinone reduction

Identifiers

PMID23201476
PMCPMC3593749
OpenAlexW2111914500

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.