Possible involvement of the 29 kDa protein in H+-ATPase in the action of cationic uncoupler of oxidative phosphorylation. Effect of the (o-phenanthroline)2-Cu2+ complex as a cationic uncoupler.

The divalent cation (o-phenanthroline)2-Cu2+ complex was found to uncouple oxidative phosphorylation in mitochondria. Its uncoupling activity depended on inorganic phosphate (Pi) in the incubation medium, and was inhibited by the SH-reagent N-ethylmaleimide, and retarded by ATP. The uncoupling by the (o-phenanthroline)2-Cu2+ complex was suggested to be due to its modification of sulfhydryl groups in the 29 kDa protein in H+-ATPase.