The Interaction between Exogenous NADH Oxidase and Succinate Oxidase in Jerusalem Artichoke (Helianthus tuberosus) Mitochondria

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Abstract
Most isolated plant mitochondria oxidize exogenous NADH via an electron transport pathway which is resistant to piericidin A and coupled to the synthesis of two molecules of ATP. Results presented show that succinate can inhibit this oxidation of added NADH. The inhibition was most marked in the absence of ADP (state 4), less obvious in the presence of added ADP (state 3), and absent in the presence of a weak acid uncoupling agent. The presence of malonate prevented the inhibition. The degree of inhibition was dependent on the concentration of succinate and appeared to be non-competitive in nature. The inhibition was shown not to be the result of the reversed flow of electrons from succinate to NAD$. The presence of external NADH appeared not to alter the rate of oxidation of succinate.

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