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• W2059821223 abstract "1. Oxidation of succinate in rat-liver mitochondria was studied in the presence of added oxaloacetate, an uncoupler of oxidative phosphorylation and rotenone. 2. At certain concentrations of oxaloacetate, succinate and mitochondria a spontaneous reactivation of succinate oxidation, previously inhibited by oxaloacetate, can be observed. This reactivation is completely abolished by either arsenate, arsenite or lewisite or by the absence of phosphate, and is potentiated by oligomycin. The spontaneous reactivation is accompanied by an increase in the intramitochondrial content of ATP generated by substrate-level phosphorylation. 3. ATP added externally reactivates the oxidation of succinate substantially only in the presence of either carnitine or, to a smaller degree, arsenate. 4. The reactivation produced by ATP plus carnitine is potentiated by the addition of small amounts of palmitate. The addition of pyruvate has a small effect and the addition of pyruvate plus arsenate almost none. 5. Freshly isolated rat-liver mitochondria contain 15–30 mμmoles free fatty acids per mg protein. This amount is increased during incubation in the presence of KCN, but during aerobic incubation with succinate fatty acids are oxidized, even if 2,4-dinitrophenol is present. 6. Upon addition of oxaloacetate the oxidation of intramitochondrial nicotinamide nucleotides is observed. The steady-state redox level depends on the concentration of added oxaloacetate and on the presence of oxidizable NAD-linked substrates. In the presence of oxaloacetate, intramitochondrial NAD(P)+ is most effectively reduced by isocitrate; ATP plus carnitine having a small effect only. 7. The best protection of succinate oxidation against the inhibition by oxaloacetate is provided by ATP plus carnitine, by ATP plus carnitine plus palmitate, or by palmitoyl-carnitine. 8. It is concluded that the oxidation of fatty acids is the most effective factor removing oxaloacetate from the site of succinate dehydrogenase in liver mitochondria. Its effect is due to (i) generation of NADH which can reduce oxaloacetate to malate, and (ii) provision of acetyl-CoA which can condense with oxaloacetate to form citrate. A smaller effectiveness of other reactions removing oxaloacetate from mitochondria is discussed." @default.
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• W2059821223 title "Inhibitory action of oxaloacetate on succinate oxidation in rat-liver mitochondria and the mechanism of its reversal" @default.
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• W2059821223 doi "https://doi.org/10.1016/0005-2728(69)90091-7" @default.
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