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Plant Physiology 65:591-594 (1980)
© 1980 American Society of Plant Biologists

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Articles

Oxidation of Reduced Nicotinamide Adenine Dinucleotide Phosphate by Potato Mitochondria

INHIBITION BY SULFHYDRYL REAGENTS 1

Geoffrey P. Arron and Gerald E. Edwards

Department of Horticulture, University of Wisconsin, Madison, Wisconsin 53706

Potato tuber mitochondria oxidized exogenous NADH and exogenous NADPH at similar rates; the electron transfer inhibitor rotenone did not inhibit the oxidation of either substrate. Submitochondrial particles, prepared from potato tuber mitochondria, exhibited a greater capacity to oxidize NADH than NADPH; rotenone inhibited the oxidation of NADH by 29% and the oxidation of NADPH by 16%. The oxidation of both NADH and NADPH by potato mitochondria exhibited pH optima of 6.8, and although substantial NADH oxidase activity was observed at pH 8.0, little NADPH oxidase activity was detected at that pH. The oxidation of NADPH by the mitochondria was more sensitive to inhibition by EDTA than was the oxidation of NADH.

The sulfhydryl reagents N-ethylmaleimide, p-chloromercuribenzoate, p-chloromercuriphenyl sulfonic acid, and mersalyl inhibited the oxidation of exogenous NADPH by the mitochondria whereas NADH oxidation was unaffected at similar concentrations of inhibitor. The data suggest that exogenous NADPH is oxidized by potato mitochondria via a dehydrogenase primarily situated on the outer face of the inner mitochondrial membrane that is neither the dehydrogenase involved with endogenous NADH oxidation nor with exogenous NADH oxidation.

1 This work was supported by the College of Agriculture and Life Sciences, University of Wisconsin, Madison, and by National Science Foundation Grant PCM 77-09384 to G. E. E.




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Copyright © 1980 by the American Society of Plant Biologists