Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.

Amandine Maréchal, Andrew M Hartley, Thomas P Warelow, Brigitte Meunier, Peter R Rich

Open access · hybridAbstract readComparative Study

In one paragraph

Article in Biochimica et biophysica acta. Bioenergetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it

0cells of the map it votes in

2citing papers in PubMed

0.5field-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

2 citing papers in PubMed, 5 citations in OpenAlex.

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
Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase.Scientific reports · 2019
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

5 authors at 4 institutions in 2 countries.

Amandine MaréchalDepartment of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, UK; Department of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK. Electronic address: a.marechal@ucl.ac.uk.

Andrew M HartleyDepartment of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, UK.

Thomas P WarelowDepartment of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK.

Brigitte MeunierInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette, France.

Peter R RichDepartment of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK. Electronic address: prr@ucl.ac.uk.

Institute of Structural and Molecular Biology · GBBirkbeck, University of London · GBUniversité Paris-Sud · FRUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H000097/1Medical Research Council MR/M00936X/1Wellcome Trust

6 · The paper itself

Abstract

Redox and CO photolysis FTIR spectra of yeast cytochrome c oxidase WT and mutants are compared to those from bovine and P. denitrificans CcOs in order to establish common functional features. All display changes that can be assigned to their E242 (bovine numbering) equivalent and to weakly H-bonded water molecules. The additional redox-sensitive band reported at 1736 cm

Indexed as

MutationAnimalsCarbon MonoxideCatalytic DomainCattleElectron Transport Complex IVKineticsLightOxidation-ReductionPhotolysisProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectroscopy, Fourier Transform InfraredCarbon MonoxideElectron Transport Complex IVSaccharomyces cerevisiae ProteinsCarboxyl groupsCytochrome c oxidaseInfrared spectroscopyMitochondriaOxidoreductionSite-directed mutagenesis

Identifiers

PMID29852141

DOI10.1016/j.bbabio.2018.05.018

PMCPMC6094048

OpenAlexW2805708885

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.