title: The complex of cytochrome c and cytochrome c peroxidase: the end of the road?
abstract: Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form a physiological complex in the inter-membrane space of yeast mitochondria, where CcP reduces hydrogen peroxide to water using the electrons provided by ferrous Cc. The Cc-CcP system has been a popular choice of study of interprotein biological electron transfer (ET) and in understanding dynamics within a protein-protein complex. In this review we have charted seven decades of research beginning with the discovery of CcP and leading to the latest functional and structural work, which has clarified the mechanism of the intermolecular ET, addressed the putative functional role of a low-affinity binding site, and identified lowly-populated intermediates on the energy landscape of complex formation. Despite the remarkable attention bestowed on this complex, a number of outstanding issues remain to be settled on the way to a complete understanding of Cc-CcP interaction.
authors.affiliation: Jean Jeener NMR Centre, Structural Biology Brussels, Vrije Universiteit Brussel, Belgium. ovolkov@vub.ac.be
authors.forename: Alexander N
authors.initials: AN
authors.lastname: Volkov
authors.forename: Peter
authors.initials: P
authors.lastname: Nicholls
authors.forename: Jonathan A R
authors.initials: JA
authors.lastname: Worrall
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003578:Cytochrome-c Peroxidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D045304:Cytochromes c / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004579:Electron Transport; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D016415:Sequence Alignment
chemical_list: D046912:Multiprotein Complexes; D045304:Cytochromes c; D003578:Cytochrome-c Peroxidase