Assembly of chloroplast cytochromes b and c.
The synthesis of holocytochromes in plastids is a catalyzed process. Several proteins, including plastid CcsA, Ccs1, possibly CcdA and a thioredoxin, plus at least two additional Ccs factors, are required in sub-stoichiometric amounts for the conversion of apocytochromes f and c(6) to their respective holoforms. CcsA, proposed to be a heme delivery factor, and Ccs1, an apoprotein chaperone, are speculated to interact physically in vivo. The formation of holocytochrome b(6) is a multi-step pathway in which at least four, as yet unidentified, Ccb factors are required for association of the b(H) heme. The specific requirement of reduced heme for in vitro synthesis of a cytochrome b(559)-derived holo-beta(2) suggests that cytochrome b synthesis in PSII might also be catalyzed in vivo.
Nakamoto
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Department of Chemistry and Biochemistry, University of California, Box 951569, Los Angeles, CA 90095-1569, USA.
Hamel
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Merchant
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D002736:Chloroplasts / Q000201:enzymology*; D003573:Cytochrome b Group / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; C068355:CcdA protein, Bacteria; D003573:Cytochrome b Group; D003574:Cytochrome c Group