ArticleThe Journal of biological chemistry2013
The heme chaperone ApoCcmE forms a ternary complex with CcmI and apocytochrome c.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation.Nature communications · 2023Article
- Architecture of the membrane-bound cytochrome c heme lyase CcmF.Nature chemical biology · 2021Article
- The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochromeThe Journal of biological chemistry · 2017Article
- During Cytochrome c Maturation CcmI Chaperones the Class I Apocytochromes until the Formation of Their b-Type Cytochrome Intermediates.The Journal of biological chemistry · 2015Article
- Cytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Biochimica et biophysica acta · 2014Review
- Engineering the assembly of heme cofactors in man-made proteins.Journal of the American Chemical Society · 2014Article
- Interaction of holoCcmE with CcmF in heme trafficking and cytochrome c biosynthesis.Journal of molecular biology · 2014Article
- Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Scientifica · 2013Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome c maturation (Ccm) is a post-translational process that occurs after translocation of apocytochromes c to the positive (p) side of energy-transducing membranes. Ccm is responsible for the formation of covalent bonds between the thiol groups of two cysteines residues at the heme-binding sites of the apocytochromes and the vinyl groups of heme b (protoporphyrin IX-Fe). Among the proteins (CcmABCDEFGHI and CcdA) required for this process, CcmABCD are involved in loading heme b to apoCcmE. The holoCcmE thus formed provides heme b to the apocytochromes. Catalysis of the thioether bonds between the apocytochromes c and heme b is mediated by the heme ligation core complex, which in Rhodobacter capsulatus contains at least the CcmF, CcmH, and CcmI components. In this work we show that the heme chaperone apoCcmE binds to the apocytochrome c and the apocytochrome c chaperone CcmI to yield stable binary and ternary complexes in the absence of heme in vitro. We found that during these protein-protein interactions, apoCcmE favors the presence of a disulfide bond at the apocytochrome c heme-binding site. We also establish using detergent-dispersed membranes that apoCcmE interacts directly with CcmI and CcmH of the heme ligation core complex CcmFHI. Implications of these findings are discussed with respect to heme transfer from CcmE to the apocytochromes c during heme ligation assisted by the core complex CcmFHI.
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