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

CcsBA is a cytochrome c synthetase that also functions in heme transport.

Proceedings of the National Academy of Sciences of the United States of America - 23 Jun 2009

Frawley Elaine R, Kranz Robert G

Abstract excerpt

Little is known about trafficking of heme from its sites of synthesis to sites of heme-protein assembly. We describe an integral membrane protein that allows trapping of endogenous heme to elucidate trafficking mechanisms. We show that CcsBA, a representative of a superfamily of integral membrane proteins involved in cytochrome c biosynthesis, exports and protects heme from oxidation. CcsBA has 10 transmembrane...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to Bacteria
Share to Core Binding Factors

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Histidine

Share to Imidazoles

Share to Ligands

Share to Lyases

Source

Open in PubMed Open full text

Identifiers

PMID: 19509336
DOI: 10.1073/pnas.0903132106
PMCID: PMC2700922

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

CcsBA is a cytochrome c synthetase that also functions in heme transport.PMID 19509336Read ↗

Structurally Mapping Endogenous Heme in the CcmCDE Membrane Complex for Cytochrome c Biogenesis.Semantic proximity Read ↗

Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein.Semantic proximity Read ↗

Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase.Semantic proximity Read ↗

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

The bacterial cell membrane acts as a dynamic heme reservoir during group B <i>Streptococcus</i> bloodstream infectionSemantic proximity Read ↗

COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase.Semantic proximity Read ↗

Membrane topology and mutational analysis of Escherichia coli CydDC, an ABC-type cysteine exporter required for cytochrome assembly.Semantic proximity Read ↗

Cyc2p, a membrane-bound flavoprotein involved in the maturation of mitochondrial c-type cytochromes.Semantic proximity Read ↗

Conserved residues of the human mitochondrial holocytochrome c synthase mediate interactions with heme.Semantic proximity Read ↗

COA8 is a COX10-binding protein involved in the early biogenesis of cytochrome c oxidaseSemantic 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 ↗

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