MEMBRANE ASSOCIATION OF THE RIESKE IRON-SULFUR PROTEIN

The mode of membrane attachment of the Rieske iron-sulfur proteins from cytochrome b(6)f complex of pea thylakoids and from cytochrome bc(1) complex of yeast mitochondria has been studied using biochemical approaches. The relative sensitivity of the Rieske protein to trypsin in the thylakoid membrane shows that all trypsin sites of the Rieske protein are on the lumen side of the thylakoid membrane. In contrast to cytochrome f the chloroplast Rieske protein was extracted from thylakoids using chaotropic agents (NaSCN, urea), an alkaline pH and relatively low concentrations of Trinon X-100. The cytochrome bc(1) complex Rieske protein from mitochondrial membranes of yeast was also released by NaSCN and alkaline treatment. The results presented here led us to the conclusion, that the mitochondrial and chloroplast Rieske proteins are extrinsic and that their association with the rest of the complex involves hydrophobic interactions.