Abstract
1. The activation energy of succinate oxidation by rat-liver mitochondria changes at a temperature of about 17° in State 3 as well as in the uncoupled state. 2. Over the whole temperature range investigated (0–23°) the rate of phosphorylation of intramitochondrial ADP during succinate oxidation exceeds that of added ADP. 3. The activation energy of the ADP-ATP and P i-ATP exchange reactions and of the 2,4-dinitrophenol-induced ATPase also changes at about 17°. 4. The temperature coefficients of the State-3 oxidation and of the P i-ATP and ADP-ATP exchange reactions are similar and, at temperatures below 17°, are high in comparison with that of the phosphorylation of intramitochondrial ADP. 5. The translocation of ADP and ATP through the inner membrane is rate-limiting for the process of oxidative phosphorylation in rat-liver mitochondria.
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