Oxygen Adaptation: THE ROLE OF THE CcoQ SUBUNIT OF THE cbb3CYTOCHROME c OXIDASE OF RHODOBACTER SPHAEROIDES 2.4.1

Abstract

The cbb(3) cytochrome c oxidase of Rhodobacter sphaeroides consists of four nonidentical subunits. Three subunits (CcoN, CcoO, and CcoP) comprise the catalytic "core" complex required for the reduction of O(2) and the oxidation of a c-type cytochrome. On the other hand, the functional role of subunit IV (CcoQ) of the cbb(3) oxidase was not obvious, although we previously suggested that it is involved in the signal transduction pathway controlling photosynthesis gene expression (Oh, J. I., and Kaplan, S. (1999) Biochemistry 38, 2688-2696). Here we go on to demonstrate that subunit IV protects the core complex, in the presence of O(2), from proteolytic degradation by a serine metalloprotease. In the absence of CcoQ, we suggest that the presence of O(2) leads to the loss of heme from the core complex, which destabilizes the cbb(3) oxidase into a "degradable" form, perhaps by altering its conformation. Under aerobic conditions the absence of CcoQ appears to affect the CcoP subunit most severely. It was further demonstrated, using a series of COOH-terminal deletion derivatives of CcoQ, that the minimum length of CcoQ required for stabilization of the core complex under aerobic conditions is the amino-terminal approximately 48-50 amino acids.