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Plant Physiology 52:622-626 (1973)
© 1973 American Society of Plant Biologists

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Articles

Regulation of Succinate Dehydrogenase in Higher Plants

II. Activation by Substrates, Reduced Coenzyme Q, Nucleotides, and Anions 1

Guillermo Oestreicher2, Patricia Hogue and Thomas P. Singer

Department of Biochemistry and Biophysics, University of California, San Francisco, California 94122, Molecular Biology Division, Veterans Administration Hospital, San Francisco, California 94121

The effect of various agents on the activation of succinate dehydrogenase in cauliflower (Brassica oleracea) and mung bean (Phaseolus aureus) mitochondria and in sonicated particles has been investigated. Reduced coenzyme Q10, inosine diphosphate, inosine triphosphate, acid pH, and anions activate the enzyme in mitochondria from higher plants in the same manner as in mammalian preparations. Significant differences have been detected in the behavior of plant and animal preparations in the effects of ATP, ADP, NADH, NAD-linked substrates, and of 2, 4-dinitrophenol on the state of activation of the dehydrogenase. In mammalian mitochondria ATP activates, whereas ADP does not, and the ATP effect is shown only in intact mitochondria. In mung bean and cauliflower mitochondria, both ATP and ADP activate and the effect is also shown in sonicated and frozen-thawed preparations. In sonicated mung bean mitochondria NADH causes complete activation, as in mammalian submitochondrial particles, but in sonicated cauliflower mitochondria activation by NADH is incomplete, as is also true of intact, anaerobic cauliflower mitochondria. Moreover, neither NAD-linked substrates nor a combination of these with NADH can fully activate the enzyme in cauliflower mitochondria. In contrast to mammalian mitochondria, succinate dehydrogenase is not deactivated in cauliflower or mung beam mitochondria under the oxidized conditions brought about by uncoupling of oxidative phosphorylation by 2,4-dinitrophenol.

2 Predoctoral Fellow of the Organization of American States, on leave of absence from the University of Chile.

1 This work was supported in part by Grant GB-36570X from the National Science Foundation.




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