Evidence map›Paper›PMID 26923069›Full record

ArticleBiochimie2016

Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure.

Andrej Musatov, Rastislav Varhač, Jonathan P Hosler, Erik Sedlák

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimie, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. A photosynthetic-respiratory electron transport chain chimera based on photosystem I and cytochromeProceedings of the National Academy of Sciences of the United States of America · 2026
    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

4 authors at 2 institutions in 2 countries.

Andrej MusatovDepartment of Biochemistry, The University of Texas Health Science Center, San Antonio, TX 78229-3900, USA; Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Košice, Slovakia. Electronic address: andrej.musatov@gmail.com.
Rastislav VarhačDepartment of Biochemistry, The University of Texas Health Science Center, San Antonio, TX 78229-3900, USA; Department of Biochemistry, P.J. Šafárik University, Moyzesova 11, 04001 Košice, Slovakia. Electronic address: rastislav.varhac@upjs.sk.
Jonathan P HoslerDepartment of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216, USA. Electronic address: jhosler@umc.edu.
Erik SedlákDepartment of Biochemistry, The University of Texas Health Science Center, San Antonio, TX 78229-3900, USA; Department of Biochemistry, P.J. Šafárik University, Moyzesova 11, 04001 Košice, Slovakia; Centre for Interdisciplinary Biosciences, P.J. Šafárik University, Jesenná 5, 04001 Košice, Slovakia. Electronic address: erik.sedlak@upjs.sk.
The University of Texas Health Science Center at San Antonio · USJackson Memorial Hospital · 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

Delipidation of detergent-solubilized cytochrome c oxidase isolated from Rhodobacter sphaeroides (Rbs-CcO) has no apparent structural and/or functional effect on the protein, however affects its resistance against thermal or chemical denaturation. Phospholipase A2 (PLA2) hydrolysis of phospholipids that are co-purified with the enzyme removes all but two tightly bound phosphatidylethanolamines. Replacement of the removed phospholipids with nonionic detergent decreases both thermal stability of the enzyme and its resilience against the effect of chemical denaturants such as urea. In contrast to nondelipidated Rbs-CcO, the enzymatic activity of PLA2-treated Rbs-CcO is substantially diminished after exposure to high (>4 M) urea concentration at room temperature without an alteration of its secondary structure. Absorbance spectroscopy and sedimentation velocity experiments revealed a strong correlation between intact tertiary structure of heme regions and quaternary structure, respectively, and the enzymatic activity of the protein. We concluded that phospholipid environment of Rbs-CcO has the protective role for stability of its tertiary and quaternary structures.

Indexed as

Protein DenaturationBacterial ProteinsElectron Transport Complex IVLipidsProtein Structure, QuaternaryRhodobacter sphaeroidesBacterial ProteinsElectron Transport Complex IVLipidsChemical denaturationDelipidationMembrane protein stabilityProtein-lipid interactionThermal denaturation

Identifiers

PMID26923069
PMCPMC4867122
OpenAlexW2281209338

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.