The enzyme holocytochrome-c synthase (EC 4.4.1.17) catalyzes the chemical reaction
holocytochrome c ⇌ {\displaystyle \rightleftharpoons } apocytochrome c + heme This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is holocytochrome-c apocytochrome-c-lyase (heme-forming). Other names in common use include cytochrome c heme-lyase, holocytochrome c synthetase, and holocytochrome-c apocytochrome-c-lyase. This enzyme participates in porphyrin and chlorophyll metabolism. Cytochrome c heme-lyase (CCHL) and cytochrome Cc1 heme-lyase (CC1HL) are mitochondrial enzymes that catalyze the covalent attachment of a heme group on two cysteine residues of cytochrome c and c1. These two enzymes are functionally and evolutionary related. There are two conserved regions, the first is located in the central section and the second in the C-terminal section. Both patterns contain conserved histidine, tryptophan and acidic residues which could be important for the interaction of the enzymes with the apoproteins and/or the heme group. The human enzyme, HCCS, processes both cytochromes c and c1.
References
Dumont ME, Ernst JF, Hampsey DM, Sherman F (1987). "Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae". EMBO J. 6 (1): 235–41. doi:10.1002/j.1460-2075.1987.tb04744.x. PMC 553382. PMID 3034577.


