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[49] Oligomycin-sensitivity-conferring protein

1979; Academic Press; Linguagem: Inglês

10.1016/0076-6879(79)55051-4

1557-7988

A.E. Senior,

Mitochondrial Function and Pathology

Publisher Summary Oligomycin-sensitivity-conferring protein (OSCP) is an interesting protein that was purified and characterized in the late 1960s and early 1970s. It is actually one subunit of the whole ATPase complex of mitochondria and it binds the F1 sector of the ATPase complex to the membrane sector of the complex. It is not the site of binding of oligomycin (or dicyclohexylcarbodiimide (DCCD)); the actual binding site of oligomycin (or DCCD) is located in the membrane part of the ATPase complex. Because soluble F1 is not oligomycin or DCCD sensitive, and membrane-bound F1 is sensitive to those inhibitors, by its action of binding F1 to the membrane, OSCP confers oligomycin sensitivity on soluble F1. OSCP has no known intrinsic enzymatic activity. However, apart from its established structural role as a connecting link between F1 and the membrane sector, OSCP also acts in the proton translocation activity of the ATPase, by conducting protons or by transmitting conformational changes that mediate uptake and release of protons.