Oxidative stress: excited oxygen species and enzyme activity.

The metabolic role of aldehydes, hydroperoxides, and quinones was investigated with emphasis on oxidative transitions involving oxygen free radicals and associated with enzymatic activities. The oxidative metabolism of aldehydes (originating either from ethanol oxidation, or monoamine oxidase activity, or oxidative breakdown of lipid hydroperoxides during lipid peroxidation) is a source of alkane production and low-level chemiluminescence. Since both parameters reflect cellular oxidative conditions, it can be inferred that side-products of aldehyde oxidase activity might participate in the link between the initial enzymatic oxidation of aldehyde and the occurrence of oxidizing species leading to chemiluminescence and alkane production. The metabolism of hydroperoxides was considered under two different aspects: first, the hydroperoxide reduction, within the frame of a detoxication mechanism, as mediated by a selenoorganic compound PZ-51 that displays glutathione peroxidase-like activity and an antioxidant activity; second, the enzyme-catalyzed disproportionation of hydroperoxides as a source of a potent oxidizing equivalent, singlet molecular oxygen. The cytotoxicity of quinones, utilized in therapeutic agents such as anticancer drugs, is believed to be related to oxidative stress due to the formation of the superoxide radical and subsequent more reactive oxygen species. The enzyme-catalyzed one-electron reduction of menadione seems to play a substantial role in the development of cytotoxic effects, at variance with the 2-electron reduction of the quinone. The observation of low-level chemiluminescence under conditions which favor the one-electron reduction process or which diminished the two-electron reduction process indicates the practicability of low-level chemiluminescence measurements in monitoring changes in quinone metabolism and related cytotoxic effects.