Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The cytochrome c maturation components CcmF, CcmH, and CcmI form a membrane-integral multisubunit heme ligation complex.

The Journal of biological chemistry - 31 Oct 2008

Sanders Carsten, Turkarslan Serdar, Lee Dong-Woo, Onder Ozlem, Kranz Robert G, Daldal Fevzi

Abstract excerpt

Cytochrome c maturation (Ccm) is a post-translational and post-export protein modification process that involves ten (CcmABCDEFGHI and CcdA or DsbD) components in most Gram-negative bacteria. The absence of any of these components abolishes the ability of cells to form cytochrome c, leading in the case of Rhodobacter capsulatus to the loss of photosynthetic proficiency and respiratory cytochrome oxidase activity....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chromatography
Share to Chromatography, Affinity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytochromes c

Share to Detergents

Share to Genetic Techniques

Share to Multiprotein Complexes

Share to Rhodobacter capsulatus

Source

Open in PubMed Open full text

Identifiers

PMID: 18753134
DOI: 10.1074/jbc.M805413200
PMCID: PMC2573057

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The cytochrome c maturation components CcmF, CcmH, and CcmI form a membrane-integral multisubunit heme ligation complex.PMID 18753134Read ↗

Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation.Semantic proximity Read ↗

The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome c maturation.Semantic proximity Read ↗

A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.Semantic proximity Read ↗

Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation.Semantic proximity Read ↗

Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB.Semantic proximity Read ↗

Features of Rhodobacter sphaeroides CcmFH.Semantic proximity Read ↗

Dynamic features of a heme delivery system for cytochrome C maturation.Semantic proximity Read ↗

Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation.Semantic proximity Read ↗

Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes.Semantic proximity Read ↗

Impact of the bacterial type I cytochrome c maturation system on different biological processes.Semantic proximity Read ↗

Transcriptional control and essential roles of the Escherichia coli ccm gene products in formate-dependent nitrite reduction and cytochrome c synthesis.Semantic proximity Read ↗

A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.