Bioenergetics in clinical medicine: prevention by forms of coenzyme Q of the inhibition by adriamycin of coenzyme Q10-enzymes in mitochondria of the myocardium.

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Abstract
The antitumor agent adriamycin inhibits the succinoxidase system and the NADH [beef heart] oxidase system. Both of the intact mitochondrial enzymes and the pentane extracted preparations are inhibited. Inhibition can be prevented by a molar ratio of coenzyme to adriamycin of 3:1 for coenzyme Q1O (ubiquinone), 5:1 for coenzyme Q7 and 5:1 for coenzyme Q4. Prevention of inhibition was observed in the decreasing order of coenzyme Q1O > coenzyme Q7 > H6 coenzyme Q4 > coenzyme Q4. Adriamycinone was 3 times more inhibitory than adriamycin, which is compatible with a less polar fragment necessary to inhibit the lipoidal coenzyme Q1O. Daunomycinone was not inhibitory at a concentration at which adriamycinone is effective, indicating that the hydroxyl group of the latter could be binding at the receptor, since it should not influence electron transfer of rings B and C.