Evidence map›Paper›PMID 25038566›Full record

ArticleBiochimie2014

Bound cardiolipin is essential for cytochrome c oxidase proton translocation.

Andrej Musatov, Neal C Robinson

Open access · greenAbstract read
In one paragraph

Article in Biochimie, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Effects of Cannabidiol on TAFAZZIN-Deficient B-Lymphoblastoid Cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Interaction of Terminal Oxidases with Amphipathic Molecules.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Review
  8. Structural basis of mammalian complex IV inhibition by steroids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. Monomeric structure of an active form of bovine cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Review
  12. Article
  13. Article
  14. Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Mitochondrial cytochrome c oxidase deficiency.Clinical science (London, England : 1979) · 2016
    Review
  17. 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

2 authors at 1 institution in 1 country.

Andrej MusatovDepartment of Biochemistry, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, TX 78229-3900, USA. Electronic address: musatov@saske.sk.
Neal C RobinsonDepartment of Biochemistry, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, TX 78229-3900, USA. Electronic address: robinson@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · US

Funding

HYDROPHOBIC ASSOCIATIONS OF MITOCHONDRIAL PROTEINSR01GM024795 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI ROBINSON, NEAL C · 1985 to 2011
$2.4M
NIGMS NIH HHS R01 GM024795
6 · The paper itself

Abstract

The proton pumping activity of bovine heart cytochrome c oxidase (CcO) is completely inhibited when all of the cardiolipin (CL) is removed from the enzyme to produce monomeric CcO containing only 11 subunits. Only dimeric enzyme containing all 13 subunits and 2-4 cardiolipin per CcO monomer exhibits a "normal" proton translocating stoichiometry of ∼1.0 H(+) per/e(-) when reconstituted into phospholipid vesicles. These fully active proteoliposomes have high respiratory control ratios (RCR = 7-15) with 75-85% of the CcO oriented with the cytochrome c binding sites exposed to the external medium. In contrast, reconstitution of CL-free CcO results in low respiratory control ratios (RCR < 5) with the enzyme randomly oriented in the vesicles, i.e., ∼50 percent oriented with the cytochrome c binding site exposed on the outside of the vesicle. Addition of exogenous CL to the CL-free enzyme completely restores electron transport activity, but restoration of proton pumping activity does not occur. This is true whether CL is added to CL-free CcO prior to reconstitution into phospholipid vesicles, or whether CL is included in the phospholipid mixture that is used to form the vesicles. Another consequence of CL removal is the inability of the 11-subunit, CL-free enzyme to dimerize upon exposure to either cholate or the cholate/PC/PE/CL mixture used during proteoliposome formation (monomeric, 13-subunit, CL-containing CcO completely dimerizes under these conditions). Therefore, a major difference between reconstitution of CL-free and CL-containing CcO is the incorporation of monomeric, rather than dimeric CcO into the vesicles. We conclude that bound CL is necessary for proper insertion of CcO into phospholipid vesicles and normal proton translocation.

Indexed as

AnimalsBinding SitesCardiolipinsCattleDimerizationElectron Transport Complex IVHydrolysisKineticsLiposomesMyocardiumPhospholipidsProton PumpsCardiolipinsElectron Transport Complex IVLiposomesPhospholipidsProton PumpsCardiolipinCytochrome c oxidaseLiposomesProton pumping

Identifiers

PMID25038566
PMCPMC4163530
OpenAlexW2028130107

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.