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The Ccm cytochrome c maturation System I catalyzes covalent attachment of heme to apocytochromes c in many bacterial species and some mitochondria. A covalent, but transient, bond between heme and a conserved histidine in CcmE along with an interaction between CcmH and the apocytochrome have been previously indicated as core aspects of the Ccm system. Here, we show that in the Ccm system from Desulfovibrio desulfuricans, no CcmH is required, and the holo-CcmE covalent bond occurs via a cysteine residue. These observations call for reconsideration of the accepted models of System I-mediated c-type cytochrome biogenesis.

Original publication

DOI

10.1074/jbc.M110.133421

Type

Journal article

Journal

J Biol Chem

Publication Date

23/07/2010

Volume

285

Pages

22882 - 22889

Keywords

Amino Acid Sequence, Bacterial Proteins, Cytochromes c, Desulfovibrio desulfuricans, Escherichia coli, Gene Deletion, Genome, Bacterial, Heme, Histidine, Models, Molecular, Molecular Sequence Data, Protein Conformation, Solubility