Studies of the oligomycin‐sensitive ATPase from yeast mitochondria. Reconstitution of ATP‐32Pi exchange in the presence of phospholipids

Abstract

A purified preparation of the oligomycin-sensitive ATPase from yeast mitochondria has been shown to elicit an oligomycin- and uncoupler-sensitive ATP-³²P_i exchange in the presence of phospholipids. Reconstitution was normally achieved by dialysis of an ATPase-phospholipid-cholate mixture. Following this procedure, vesicles with diameters between 200 and 1,500 Å were seen by electron microscopy. As in mitochondria, ATPase activity in the reconstituted system was stimulated by a range of uncouplers which inhibited ATP-³²P_i exchange. These and other findings suggest that the coupling mechanism may still be intact within the ATPase complex.