Abstract
Holocytochrome c synthase (HCCS) attaches heme covalently to mitochondrial respiratory cytochromes c. Little is known about the reaction of heme attachment to apocytochromes c by HCCS, although recently it has been established that the CXXCH motif and the N‐terminus of the apocytochrome polypeptide are important protein–protein recognition motifs. Here, we explore further the important features of the N‐terminal sequence and investigate what variations in the CXXCH residues are productively recognised by HCCS in its substrate.

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