Abstract
During inhibition of oxidative phosphorylation by oligomycin, palmitoyl-CoA (p-CoA) reduces the velocity of energy-dependent reduction of acetoacetate and the Ca++-capacity of the mitochondria in medium with phosphate. Energy-independent osmotic swelling of the mitochondria in medium with NH4NO3, which depends on the proton conductance of the inner membrane, is inhibited by ADP and accelerated by p-CoA. All effects of p-CoA are abolished by carnitine and competitively by ADP. It is concluded that the lowering of the energization level by p-CoA is connected with increased permeability of the inner membrane for H+ as a result of binding of the inhibitor with adenine-nucleotide translocase.
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