Studies on the relationship between ATP synthesis and transport and the proton electrochemical gradient in rat liver mitochondria.
The effect of ATP synthesis on delta mu H in rat liver mitochondria has been analyzed by separating the steps of adenine nucleotide translocation and ATP synthesis in the matrix. Either exchange of ATP, synthesized by substrate level phosphorylation in the matrix of oligomycin-treated mitochondria, for external ADP, or activity of the membrane-bound ATP synthase complex results in delta mu H depression with respect to resting state levels. This depression appears to be more pronounced, under strictly comparable conditions, when arsenate is used to stimulate ATP synthase activity than when the ornithine-citrulline conversion reaction is used for the same purpose.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D000818:Animals; D001149:Arsenates / Q000378:metabolism; D001692:Biological Transport; D008297:Male; D008930:Mitochondria, Liver / Q000378:metabolism*; D009952:Ornithine / Q000378:metabolism; D010101:Oxygen Consumption; D006180:Proton-Translocating ATPases; D051381:Rats; D011919:Rats, Inbred Strains; D013816:Thermodynamics
D001149:Arsenates; D000255:Adenosine Triphosphate; D009952:Ornithine; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases