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Mmicular mechanisms of cytochrome c biogenesis: three distinct systems
Author(s) -
Kranz Robert,
Lill Roland,
Goldman Barry,
Bonnard Géraldine,
Merchant Sabeeha
Publication year - 1998
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1998.00869.x
Subject(s) - biology , biogenesis , biochemistry , cytochrome , mitochondrion , cytochrome c , intermembrane space , gene , enzyme , bacterial outer membrane , escherichia coli
The past 10 years have heralded remarkable progress in the understanding of the biogenesis of c ‐type cytochromes. The hallmark of c ‐type cytochrome synthesis is the covalent ligation of haem vinyl groups to two cysteinyl residues of the apocytochrome (at a Cys–Xxx–Yyy–Cys–His signature motif). From genetic, genomic and biochemical studies, it is clear that three distinct systems have evolved in nature to assemble this ancient protein. In this review, common principles of assembly for all systems and the mmicular mechanisms predicted for each system are summarized. Prokaryotes, plant mitochondria and chloroplasts use either system I or II, which are each predicted to use dedicated mechanisms for haem delivery, apocytochrome ushering and thioreduction. Accessory proteins of systems I and II co‐ordinate the positioning of these two substrates at the membrane surface for covalent ligation. The third system has evolved specifically in mitochondria of fungi, invertebrates and vertebrates. For system III, a pivotal role is played by an enzyme called cytochrome c haem lyase (CCHL) in the mitochondrial intermembrane space.