Inhibition by adenine derivatives of the cyanide-insensitive electron transport pathway of plant mitochondria.

The effect of benzylaminopurine was studied on cyanide-resistant mitochondria isolated from aged slices of potato tuber (Solanum tuberosum L. var. Bintje). Benzylaminopurine specifically acted on the cyanide-resistant alternative pathway. In the case of succinate oxidation, it mimicked the action of salicylhydroxamic acid and restored a good oxidative phosphorylation. Kinetic analyses showed that inhibitions by benzylaminopurine, salicylhydroxamic acid, and disulfiram occurred at mutually exclusive sites on the alternative pathway. Cyanide-resistant malate oxidation was only partially inhibited by benzylaminopurine and this inhibition occurred for low concentrations of this compound. On the other hand, the oxidation of exogenous NADH remained unaffected.The effects of several adenine derivatives with or without cytokinin activity and that of a purine analog with anticytokinin activity were also studied. The variation in effectiveness to inhibit cyanide-resistant electron transport was: benzylaminopurine and 7-pentylamino-3-methylpyrazolo (4,3 d) pyrimidine (anticytokinin) > alpha-alpha' dimethyl-allyl-adenine > 6-benzoylamino-9-benzylpurine > kinetin > adenine. No correlation was observed between the ability to inhibit the alternative pathway and the biological activity of these compounds. Liposolubility appeared as a major factor for potential inhibitory effect on the alternative pathway.