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lüll Cytochrome c biogenesis: the Ccm system Sanders C; Turkarslan S; Lee DW; Daldal FTrends Microbiol 2010[Jun]; 18 (6): 266-74Cytochromes of c-type contain covalently attached hemes that are formed via thioether bonds between the vinyls of heme b and cysteines within C(1)XXC(2)H 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 approximately Cys(1) and vinyl-4 approximately Cys(2) heme b-apocytochrome thioether bonds in c-type cytochromes.|Archaea/*metabolism[MESH]|Archaeal Proteins/metabolism[MESH]|Bacteria/*metabolism[MESH]|Bacterial Outer Membrane Proteins/metabolism[MESH]|Bacterial Proteins/metabolism[MESH]|Cysteine/chemistry/metabolism[MESH]|Cytochromes c/*chemistry/*metabolism[MESH]|Heme/chemistry/metabolism[MESH]|Mitochondria/*metabolism[MESH]|Plant Proteins/metabolism[MESH]|Plants/metabolism[MESH]|Protein Processing, Post-Translational[MESH]|Rhodophyta/*metabolism[MESH]|Sulfides/chemistry/metabolism[MESH] |