Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3422267 | Trends in Microbiology | 2010 | 9 Pages |
Abstract
Cytochromes of c-type contain covalently attached hemes that are formed via thioether bonds between the vinyls of heme b and cysteines within C1XXC2H motifs of apocytochromes. In diverse organisms this post-translational modification relies on membrane-associated specific biogenesis proteins, referred to as cytochrome c maturation (Ccm) systems. A highly complex version of these systems, Ccm or System I, is found in Gram-negative bacteria, archaea and plant mitochondria. We describe emerging functional interactions between the Ccm components categorized into three conserved modules, and present a mechanistic view of the molecular basis of ubiquitous vinyl-2∼Cys1 and vinyl-4∼Cys2 heme b–apocytochrome thioether bonds in c-type cytochromes.
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Authors
Carsten Sanders, Serdar Turkarslan, Dong-Woo Lee, Fevzi Daldal,