Cytochrome c biogenesis: the Ccm system.
Cytochromes 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.
Sanders
Carsten
C
Kutztown University, Department of Biology, Kutztown, PA 19530, USA.
Turkarslan
Serdar
S
Lee
Dong-Woo
DW
Daldal
Fevzi
F
D001105:Archaea / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism; D010944:Plants / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D000461:Rhodophyta / Q000378:metabolism*; D013440:Sulfides / Q000737:chemistry / Q000378:metabolism
D019843:Archaeal Proteins; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D010940:Plant Proteins; D013440:Sulfides; D006418:Heme; D045304:Cytochromes c; D003545:Cysteine
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