Disparate pathways for the biogenesis of cytochrome oxidases in Bradyrhizobium japonicum.

ABSTRACT: This work addresses the biogenesis of heme-copper terminal oxidases in Bradyrhizobium japonicum, the nitrogen-fixing root nodule symbiont of soybean. B. japonicum has four quinol oxidases and four cytochrome oxidases. The latter include the aa(3)- and cbb(3)-type oxidases. Although both have a Cu(B) center in subunit I, the subunit II proteins differ in having either a Cu(A) center (in aa(3)) or a covalently bound heme c (in cbb(3)). Two biogenesis factors were genetically studied here, the periplasmically exposed CoxG and ScoI proteins, which are the respective homologs of the mitochondrial copper-trafficking chaperones Cox11 and Sco1 for the formation of the Cu(B) center in subunit I and the Cu(A) center in subunit II of cytochrome aa(3). We could demonstrate copper binding to ScoI in vi

SUBMITTER: Buhler D 

PROVIDER: S-EPMC2871436 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature