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The covalent attachment of heme to mitochondrial cytochrome c is catalysed by holocytochrome c synthase (HCCS, also called heme lyase). How HCCS functions and recognises the substrate apocytochrome is unknown. Here we have examined HCCS recognition of a chimeric substrate comprising a short mitochondrial cytochrome c N-terminal region with the C-terminal sequence, including the CXXCH heme-binding motif, of a bacterial cytochrome c that is not otherwise processed by HCCS. Heme attachment to the chimera demonstrates the importance of the N-terminal region of the cytochrome. A series of variants of a mitochondrial cytochrome c with amino acid replacements in the N-terminal region have narrowed down the specificity determinants, providing insight into HCCS substrate recognition.

Original publication

DOI

10.1016/j.febslet.2011.04.058

Type

Journal article

Journal

FEBS Lett

Publication Date

23/06/2011

Volume

585

Pages

1891 - 1896

Keywords

Amino Acid Sequence, Bacterial Proteins, Binding Sites, Cytochromes c, Heme, Holoenzymes, Lyases, Mitochondrial Proteins, Substrate Specificity