Evidence map›Paper›PMID 25372183›Full record

ArticleThe journal of physical chemistry. B2015

Identification of ubiquinol binding motifs at the Qo-site of the cytochrome bc1 complex.

Angela M Barragan, Antony R Crofts, Klaus Schulten, Ilia A Solov'yov

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Flexibility and Hydration of the QJournal of chemical information and modeling · 2025
    Article
  5. Article
  6. The cytochrome bPhotosynthesis research · 2024
    Review
  7. CoQAntioxidants (Basel, Switzerland) · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  14. Article
  15. Article
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  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

4 authors at 2 institutions in 3 countries.

Angela M BarraganDepartment of Physics, University of Illinois at Urbana-Champaign , 1110 W. Green Street, Urbana, Illinois 61801, United States.
Antony R Crofts
Klaus Schulten
Ilia A Solov'yov
University of Illinois Urbana-Champaign · USUniversity of Southern Denmark · DK

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
MOLECULAR ARCHITECTURE OF UQH2: CYTC2 OXIDOREDUCTASER01GM035438 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI CROFTS, ANTONY R. · 1986 to 2011
$3.3M
NIGMS NIH HHS 1 R01 GM067887NIGMS NIH HHS 9P41GM104601NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM035438NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01 GM35438
6 · The paper itself

Abstract

Enzymes of the bc1 complex family power the biosphere through their central role in respiration and photosynthesis. These enzymes couple the oxidation of quinol molecules by cytochrome c to the transfer of protons across the membrane, to generate a proton-motive force that drives ATP synthesis. Key for the function of the bc1 complex is the initial redox process that involves a bifurcated electron transfer in which the two electrons from a quinol substrate are passed to different electron acceptors in the bc1 complex. The electron transfer is coupled to proton transfer. The overall mechanism of quinol oxidation by the bc1 complex is well enough characterized to allow exploration at the atomistic level, but details are still highly controversial. The controversy stems from the uncertain binding motifs of quinol at the so-called Qo active site of the bc1 complex. Here we employ a combination of classical all atom molecular dynamics and quantum chemical calculations to reveal the binding modes of quinol at the Qo-site of the bc1 complex from Rhodobacter capsulatus. The calculations suggest a novel configuration of amino acid residues responsible for quinol binding and support a mechanism for proton-coupled electron transfer from quinol to iron-sulfur cluster through a bridging hydrogen bond from histidine that stabilizes the reaction complex.

Indexed as

Amino Acid MotifsElectron TransportElectron Transport Complex IIIMolecular Dynamics SimulationProtein BindingQuantum TheoryRhodobacter capsulatusUbiquinoneWaterElectron Transport Complex IIIubiquinolUbiquinoneWater

Identifiers

PMID25372183
PMCPMC4297238
OpenAlexW2418755576

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.