[Effect of palmitoyl-CoA binding with adenine nucleotide translocase on energization of mitochondria].

Under conditions of inhibiting oxidative phosphorylation of oligomycin palmitoyl-CoA (p-CoA) decreases the rate of energy dependent reduction of acetoacetate and Ca2+-capacity of mitochondria in a phosphate medium. Energy independent osmotic swelling of mitochondria in NH4NO3, which depends on H+ permeability of the inner mitochondrial membrane is inhibited by ADP and acclereated by p-CoA. Carnitin and competitive ADP abolish all the effects of p-CoA. It is concluded that decreased energization induced by p-CoA is related to an increase in the inner mitochondrial membrane permeability b- H+ as a result of the inhibitor bindings with adenine nucleotide translocase.