In many bacteria the ccoGHIS cluster, located immediately downstream of the
structural genes (ccoNOQP) of cytochrome cbb(3) oxidase, is required for t
he biogenesis of this enzyme. Genetic analysis of ccoGHIS in Rhodobacter Ca
psulatus demonstrated that ccoG, ccoH, ccoI and ccoS are expressed independ
ently of each other, and do not form a simple operon. Absence of CcoG, whic
h has putative (4Fe-4S) cluster binding motifs, does not significantly affe
ct cytochrome cbb(3) oxidase activity. However, CcoH and CcoI are required
for normal steady-state amounts of the enzyme. CcoI is highly homologous to
ATP-dependent metal ion transporters, and appears to be involved in the ac
quisition of copper for cytochrome cbb(3) oxidase, since a CcoI-minus pheno
type could be mimicked by copper ion starvation of a wild-type strain. Rema
rkably, the small protein CcoS, with a putative single transmembrane span,
is essential for the incorporation of the redox-active prosthetic groups (h
eme b, heme b(3) and Cu) into the cytochrome cbb(3) oxidase. Thus, the ccoC
HIS products are involved in several steps during the maturation of the cyt
ochrome cbb(3) oxidase. (C) 2000 Academic Press.