Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1793, Issue 1, Pages 125-138Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2008.06.017
Keywords
Mitochondria; Cytochrome c assembly; Thioether linkage; Heme transport; Heme lyase; Redox chemistry
Categories
Funding
- Muscular Dystrophy Association [MDA 4247]
- College of Biological Sciences
- College of Medicine
- Dorothy M. Davis Heart and Lung Institute at The Ohio State University
- American Heart Association
- Centre National de la Recherche Scientifique
- Marie Curie
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Cytochromes c are metalloproteins that function in electron transfer reactions and contain a heme moiety covalently attached via thioether linkages between the co-factor and a CXXCH motif in the protein. Covalent attachment of the heme group occurs on the positive side of all energy-transducing membranes (bacterial periplasm, mitochondrial intermembrane space and thylakoid lumen) and requires minimally: 1) synthesis and translocation of the apocytochromes c and heme across at least one biological membrane, 2) reduction of apocytochromes c and heme and maintenance under a reduced form prior to 3) catalysis of the heme attachment reaction. Surprisingly, the conversion of apoforms of cytochromes c to their respective holoforms occurs through at least three different pathways (systems I, II and III). In this review, we detail the assembly process of soluble cytochrome c and membrane-bound cytochrome cl, the only two mitochondrial c-type cytochromes that function in respiration. Mitochondrial c-type cytochromes are matured in the intermembrane space via the system I or system III pathway, an intriguing finding considering that the biochemical requirements for cytochrome c maturation are believed to be common regardless of the energy-transducing membrane under study. Published by Elsevier B.V.
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