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.
D000818:Animals; D007700:Kinetics; D046911:Macromolecular Substances; D008297:Male; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D010085:Oxidative Phosphorylation / Q000187:drug effects*; D010618:Phenanthrolines / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014475:Uncoupling Agents / Q000494:pharmacology*
D046911:Macromolecular Substances; D010618:Phenanthrolines; D014475:Uncoupling Agents; C014741:bis(1,10-phenanthroline)copper(2+) ion; D006180:Proton-Translocating ATPases