Evidence map›Paper›PMID 26775610›Full record

ArticleJournal of inorganic biochemistry2016

Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability.

Matthew E Goldes, Margaret E Jeakins-Cooley, Levi J McClelland, Tung-Chung Mou, Bruce E Bowler

Open access · greenAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-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

12 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Human CytochromeBiochemistry · 2020
    Article
  7. Naturally Occurring A51V Variant of Human CytochromeThe journal of physical chemistry. B · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Journal of the American Chemical Society · 2016
    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.

Matthew E GoldesDepartment of Chemistry and Biochemistry, University of Montana, Missoula, MT 59812, United States.
Margaret E Jeakins-CooleyDepartment of Chemistry and Biochemistry, University of Montana, Missoula, MT 59812, United States.
Levi J McClellandDepartment of Chemistry and Biochemistry, University of Montana, Missoula, MT 59812, United States; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT 59812, United States.
Tung-Chung MouDivision of Biological Sciences, University of Montana, Missoula, MT 59812, United States; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT 59812, United States.
Bruce E BowlerDepartment of Chemistry and Biochemistry, University of Montana, Missoula, MT 59812, United States; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT 59812, United States. Electronic address: bruce.bowler@umontana.edu.
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
NIGMS NIH HHS P20 GM103546
6 · The paper itself

Abstract

The hypothesis that the recent rapid evolution of primate cytochromes c, which primarily involves residues in the least stable Ω-loop (Ω-loop C, residues 40-57), stabilizes the heme crevice of cytochrome c relative to other mammals, is tested. To accomplish this goal, we have compared the properties of human and spider monkey cytochrome c and a set of four variants produced in the process of converting human cytochrome c into spider monkey cytochrome c. The global stability of all variants has been measured by guanidine hydrochloride denaturation. The stability of the heme crevice has been assessed with the alkaline conformational transition. Structural insight into the effects of the five amino acid substitutions needed to convert human cytochrome c into spider monkey cytochrome c is provided by a 1.15Å resolution structure of spider monkey cytochrome c. The global stability for all variants is near 9.0kcal/mol at 25°C and pH7, which is higher than that observed for other mammalian cytochromes c. The heme crevice stability is more sensitive to the substitutions required to produce spider monkey cytochrome c with decreases of up to 0.5 units in the apparent pKa of the alkaline conformational transition relative to human cytochrome c. The structure of spider monkey cytochrome c indicates that the Y46F substitution destabilizes the heme crevice by disrupting an extensive hydrogen bond network that connects three surface loops including Ω-loop D (residues 70-85), which contains the Met80 heme ligand.

Indexed as

Amino Acid SubstitutionAnimalsAtelinaeCircular DichroismCrystallography, X-RayCytochromes cHemeHumansHydrogen BondingHydrogen-Ion ConcentrationKineticsProtein FoldingProtein StabilityCytochromes cHemeAlkaline conformational transitionGlobal stabilityHeme crevice stabilityHydrogen bond networkSpider monkey cytochrome c

Identifiers

PMID26775610
PMCPMC4887337
OpenAlexW2210811658

What OpenQuestion holds

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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.