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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.

Original publication

DOI

10.1016/j.febslet.2014.07.026

Type

Journal article

Journal

FEBS Lett

Publication Date

17/09/2014

Volume

588

Pages

3367 - 3374

Keywords

Ccm system, Cytochrome c, Heme, Holocytochrome c synthase, Amino Acid Sequence, Amino Acid Substitution, Animals, Conserved Sequence, Cytochromes c, Horses, Lyases, Mitochondrial Proteins, Molecular Sequence Data, Protein Binding, Saccharomyces cerevisiae Proteins