Evidence map›Paper›PMID 28598148›Full record

ArticleBiochemistry2017

Effect of a K72A Mutation on the Structure, Stability, Dynamics, and Peroxidase Activity of Human Cytochrome c.

Shiloh M Nold, Haotian Lei, Tung-Chung Mou, Bruce E Bowler

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. A Divergent CytochromebioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. The Increase in the Peroxidase Activity of the CytochromeInternational journal of molecular sciences · 2024
    Article
  7. Review
  8. Article
  9. Alkaline State of the Domain-Swapped Dimer of Human CytochromeJournal of the American Chemical Society · 2022
    Article
  10. Article
  11. Article
  12. The Human CytochromeBiochemistry · 2020
    Article
  13. Article
  14. Review
  15. Naturally Occurring A51V Variant of Human CytochromeThe journal of physical chemistry. B · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. 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 1 institution in 1 country.

Shiloh M NoldDepartment of Chemistry and Biochemistry, University of Montana , Missoula, Montana 59812, United States.
Haotian LeiDepartment of Chemistry and Biochemistry, University of Montana , Missoula, Montana 59812, United States.
Tung-Chung MouDivision of Biological Sciences, University of Montana , Missoula, Montana 59812, United States.
Bruce E BowlerDepartment of Chemistry and Biochemistry, University of Montana , Missoula, Montana 59812, United States.ORCID 0000-0003-1543-2466
University of Montana · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
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
NIGMS NIH HHS P20 GM103546NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

We test the hypothesis that Lys72 suppresses the intrinsic peroxidase activity of human cytochrome c, as observed previously for yeast iso-1-cytochrome c [McClelland, L. J., et al. (2014) Proc. Natl. Acad. Sci. U. S. A. 111, 6648-6653]. A 1.25 Å X-ray structure of K72A human cytochrome c shows that the mutation minimally affects structure. Guanidine hydrochloride denaturation demonstrates that the K72A mutation increases global stability by 0.5 kcal/mol. The K72A mutation also increases the apparent pK

Indexed as

Models, MolecularAmino Acid SubstitutionBiocatalysisCatalytic DomainCrystallography, X-RayCytochromes cDatabases, ProteinEnzyme StabilityHumansHydrogen-Ion ConcentrationKineticsLysineMutagenesis, Site-DirectedMutationPeroxidasesProtein ConformationCYC1 protein, S cerevisiaeCytochromes cLysinePeroxidasesRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID28598148
PMCPMC5564420
OpenAlexW2623695165

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.