Evidence map›Paper›PMID 24760830›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity.

Levi J McClelland, Tung-Chung Mou, Margaret E Jeakins-Cooley, Stephen R Sprang, Bruce E Bowler

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A Divergent CytochromebioRxiv : the preprint server for biology · 2025
    Article
  6. Chemical propulsion of hemozoin crystal motion in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. The Increase in the Peroxidase Activity of the CytochromeInternational journal of molecular sciences · 2024
    Article
  11. Direct tests of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Alkaline State of the Domain-Swapped Dimer of Human CytochromeJournal of the American Chemical Society · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Interactions between mitochondria-damaging platinum(IV) prodrugs and cytochrome c.Dalton transactions (Cambridge, England : 2003) · 2022
    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 1 institution in 1 country.

Levi J McClellandDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, and Division of Biological Sciences, University of Montana, Missoula, MT 59812.
Tung-Chung Mou
Margaret E Jeakins-Cooley
Stephen R Sprang
Bruce E Bowler
University of Montana · US

Funding

Surveillance genome sequencing to detect SARS-CoV-2 virus variants in MontanaP20GM103546 · NIGMS · UNIVERSITY OF MONTANA · PI BOWLER, BRUCE E · 2012 to 2021
$19.2M
IMMUNOGENETIC STUDIES OF THE HUMAN MHCR01GM010356 · NIGMS · DUKE UNIVERSITY · PI WARD, FRANCES E · 1985 to 1989
–
NIGMS NIH HHS P20 GM103546NIGMS NIH HHS P20GM10356
6 · The paper itself

Abstract

At the onset of apoptosis, the peroxidation of cardiolipin at the inner mitochondrial membrane by cytochrome c requires an open coordination site on the heme. We report a 1.45-Å resolution structure of yeast iso-1-cytochrome c with the Met80 heme ligand swung out of the heme crevice and replaced by a water molecule. This conformational change requires modest adjustments to the main chain of the heme crevice loop and is facilitated by a trimethyllysine 72-to-alanine mutation. This mutation also enhances the peroxidase activity of iso-1-cytochrome c. The structure shows a buried water channel capable of facilitating peroxide access to the active site and of moving protons produced during peroxidase activity to the protein surface. Alternate positions of the side chain of Arg38 appear to mediate opening and closing of the buried water channel. In addition, two buried water molecules can adopt alternate positions that change the network of hydrogen bonds in the buried water channel. Taken together, these observations suggest that low and high proton conductivity states may mediate peroxidase function. Comparison of yeast and mammalian cytochrome c sequences, in the context of the steric factors that permit opening of the heme crevice, suggests that higher organisms have evolved to inhibit peroxidase activity, providing a more stringent barrier to the onset of apoptosis.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionApoptosisCrystallography, X-RayCytochromes cElectron TransportHemeHydrogen BondingLipid PeroxidationMitochondriaModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeroxidaseProtein ConformationSaccharomyces cerevisiaeCYC1 protein, S cerevisiaeCytochromes cHemePeroxidaseSaccharomyces cerevisiae Proteins

Identifiers

PMID24760830
PMCPMC4020089
OpenAlexW2003513216

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.