Evidence map›Paper›PMID 22121193›Full record

ArticleThe Journal of biological chemistry2012

A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.

Despoina A I Mavridou, Julie M Stevens, Leonie Mönkemeyer, Oliver Daltrop, Katalin di Gleria, Benedikt M Kessler, Stuart J Ferguson, James W A Allen

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. The CcmC-CcmE interaction during cytochromeThe Journal of biological chemistry · 2018
    Article
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  4. Review
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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

8 authors.

Despoina A I MavridouDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Julie M Stevens
Leonie Mönkemeyer
Oliver Daltrop
Katalin di Gleria
Benedikt M Kessler
Stuart J Ferguson
James W A Allen

Funding

Biotechnology and Biological Sciences Research Council BB/D019753/1Biotechnology and Biological Sciences Research Council BB/H017887/1Wellcome Trust 092532
6 · The paper itself

Abstract

c-Type cytochromes are widespread proteins, fundamental for respiration or photosynthesis in most cells. They contain heme covalently bound to protein in a highly conserved, highly stereospecific post-translational modification. In many bacteria, mitochondria, and archaea this heme attachment is catalyzed by the cytochrome c maturation (Ccm) proteins. Here we identify and characterize a covalent, ternary complex between the heme chaperone CcmE, heme, and cytochrome c. Formation of the complex from holo-CcmE occurs in vivo and in vitro and involves the specific heme-binding residues of both CcmE and apocytochrome c. The enhancement and attenuation of the amounts of this complex correlates completely with known consequences of mutations in genes for other Ccm proteins. We propose the complex is a trapped catalytic intermediate in the cytochrome c biogenesis process, at the point of heme transfer from CcmE to the cytochrome, the key step in the maturation pathway.

Indexed as

Bacterial Outer Membrane ProteinsCytochromes cEscherichia coliEscherichia coli ProteinsHemeHemeproteinsMultiprotein ComplexesProtein BiosynthesisBacterial Outer Membrane ProteinsCcmE protein, E coliCytochromes cEscherichia coli ProteinsHemeHemeproteinsMultiprotein Complexes

Identifiers

PMID22121193
PMCPMC3268396

What OpenQuestion holds

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Registered trials

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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.