Abstract

Oxidation of 2-oxoglutarate (in the presence of malonate) by mitochondria isolated from turnip, pea leaf and cauliflower tissue was dramatically inhibited by micromolar concentrations of pyruvate. Pyruvate, however, had little or no effect on 2-OG oxidation when carried out in the absence of malonate. The inhibition was reversed by α-cyano-4-hydroxycinnamic acid, indicating pyruvate uptake into the matrix was required for the inhibitory effect. In contrast, pyruvate had no effect on 2-oxoglutarate oxidation by mitochondria isolated from rat heart. The possible significance of the effect in terms of the control of 2-oxo-glutarate dehydrogenase activity during the operation of a malate / aspartate shuttle in plant mitochondria is discussed.

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