Evidence map›Paper›PMID 22066495›Full record

ArticleBiochemistry2011

Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF.

Brian San Francisco, Eric C Bretsnyder, Kenton R Rodgers, Robert G Kranz

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

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  6. Maize PPR278 Functions in Mitochondrial RNA Splicing and Editing.International journal of molecular sciences · 2022
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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 1 country.

Brian San FranciscoDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri 63130, United States.
Eric C Bretsnyder
Kenton R Rodgers
Robert G Kranz
Washington University in St. Louis · USNorth Dakota State University · US

Funding

MOLECULAR GENETIC ANALYSES OF CYTOCHROMES C BIOGENESISR01GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1994 to 2019
$6.0M
Study of heme uptake and transport proteins from P. aerugenosa and S. dysenteriaeR15AI072719 · NIAID · NORTH DAKOTA STATE UNIVERSITY · PI RODGERS, KENTON · 2007 to 2011
$707k
CYTOCHROMES C BIOGENESISR55GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1992 to 1992
–
NIAID NIH HHS AI072719NIAID NIH HHS R15 AI072719NIGMS NIH HHS GM47909NIGMS NIH HHS R01 GM047909
6 · The paper itself

Abstract

Cytochrome c maturation in many bacteria, archaea, and plant mitochondria involves the integral membrane protein CcmF, which is thought to function as a cytochrome c synthetase by facilitating the final covalent attachment of heme to the apocytochrome c. We previously reported that the E. coli CcmF protein contains a b-type heme that is stably and stoichiometrically associated with the protein and is not the heme attached to apocytochrome c. Here, we show that mutation of either of two conserved transmembrane histidines (His261 or His491) impairs stoichiometric b-heme binding in CcmF and results in spectral perturbations in the remaining heme. Exogeneous imidazole is able to correct cytochrome c maturation for His261 and His491 substitutions with small side chains (Ala or Gly), suggesting that a "cavity" is formed in these CcmF mutants in which imidazole binds and acts as a functional ligand to the b-heme. The results of resonance Raman spectroscopy on wild-type CcmF are consistent with a hexacoordinate low-spin b-heme with at least one endogeneous axial His ligand. Analysis of purified recombinant CcmF proteins from diverse prokaryotes reveals that the b-heme in CcmF is widely conserved. We have also determined the reduction potential of the CcmF b-heme (E(m,7) = -147 mV). We discuss these results in the context of CcmF structure and functions as a heme reductase and cytochrome c synthetase.

Indexed as

Amino Acid SubstitutionBinding SitesBiocatalysisEnzyme ActivationEscherichia coli ProteinsHemeHistidineHoloenzymesImidazolesIndicators and ReagentsLigandsLyasesModels, MolecularMutant ProteinsOxidation-ReductionPhylogenycytochrome C synthetaseEscherichia coli ProteinsHemeHistidineHoloenzymesimidazoleImidazolesIndicators and ReagentsLigandsLyasesMutant ProteinsProtein SubunitsRecombinant Proteins

Identifiers

PMID22066495
PMCPMC3237939
OpenAlexW2086318858

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.