[Octanol oxidation by the mitochondria of Torulopsis candida]

Octanol oxidation by the mitochondria of Torulopsis candida grown on hexadecane was studied. Octanol oxidation involves an enzyme system labile to heating but resistant to the main inhibitors of the phosphorylating respiration chain. When octanol is oxidized in aerobic conditions, cytochrome b is reduced, with the absorption maxima in alpha, beta and gamma bands being at 555, 526 and 425 nm, respectively. The cytochrome is reduced in aerobic conditions also in the presence of exogenous NADH and rotenone. In contrast to octanol oxidation, oxidation of the aldehyde C9 by mitochondria was sensitive to the action of inhibitors of the respiration chain and phosphorylation. When the aldehyde C9 is oxidized, cytochrome b is reduced, with the absorption maxima in alpha, beta and gamma bands being at 562, 530 and 433 nm, respectively. The results are indicative of the fact that different electron transport chains are involved in the transport of reducing equivalents from higher alcohols and aldehydes oxidized by mitochondria: in the first case, the NADH--cytochrome b5 reductase chain, and in the second case, the main phosphorylating electron transport chain.