Article ID Journal Published Year Pages File Type
3422267 Trends in Microbiology 2010 9 Pages PDF
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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