SOME RECENT ADVANCES RELATING TO PROKARYOTIC CYTOCHROME-C REDUCTASES AND CYTOCHROME-C OXIDASES

Prokaryotic systems provide excellent experimental opportunities for exploring structure/function relationships for the complex, membrane-bound, multisubunit enzymes responsible for the reduction and subsequent oxidation of c-type cytochromes in respiratory or photosynthetic electron transport chains. Two points are made in this mini-review: (1) The eukaryotic and prokaryotic aa3-type cytochrome c oxidases are members of an apparently large superfamily of structurally related respiratory oxidases. This superfamily displays considerable variation in terms of the heme prosthetic groups (a or b) as well as the substrate oxidized (quinol or cytochrome c). The relationships among these enzymes help to facilitate explorations of how they work. (2) Molecular biology techniques can be used to generate intact, redox-active, water-soluble domains of membrane-bound subunits. These soluble domains can be used for detailed examination, including obtaining high resolution structure by NMR techniques or by X-ray crystallography. This approach is being used to study the soluble heme-binding domain of cytochrome c1 from the bc1 complex of Rhodobacter sphaeroides.