Endogenous and exogenous regulation of redox-properties of coenzyme Q

Ubiquinol (QH2, reduced coenzyme Q) is increasingly reported to exert antioxidant functions besides its implication in mitochondrial energy metabolism. On the other hand ubisemiquinones (SQ-.) of the respiratory chain are considered to account for the production of superoxide radicals as a byproduct of cellular respiration. Since the formation of potentially prooxidative ubisemiquinones can be expected to result from the antioxidant activity of ubiquinol, the evaluation whether or not QH2 exerts antioxidant activities depends on the fate of antioxidant-derived metabolites and the existence of a natural recycling system for oxidized QH2. We have recently shown that SQ increasingly undergo autoxidation when approaching the external more polar phase of the membrane. In contrast to mitochondria where the QH2/ SQ-./Q pools are dynamically kept in relatively stable relationships the fate of semi and fully oxidized QH2 is not at all clear in LDL particles where QH2 is suggested to exert important antioxidant functions. Therefore, the antioxidant-derived metabolites of QH2 in liposomes following lipid peroxidation were studied with respect to their localization in the bilayer and the possibility to recycle oxidized QH2 via dihydrolipoic acid (DHLA). The results revealed a considerable fraction of QH2 existing in the outer membrane section where protons from the aqueous phase have access to allow autoxidation. DHLA was found to recycle oxidized QH2 although due to slow partition equilibration the reduction velocity appears to be not sufficient for therapeutic application.