Distribution of tocopheryl quinone in mitochondrial membranes and interference with ubiquinone-mediated electron transfer

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Abstract

α-Tocopherol (Toc) is an efficient lipophilic antioxidant present in all mammalian lipid membranes. This chromanol is metabolized by two different pathways: excessive dietary Toc is degraded in the liver by side chain oxidation, and Toc acting as antioxidant is partially degraded to α-tocopheryl quinone (TQ). The latter process and the similarity between TQ and ubiquinone (UQ) prompted us to study the distribution of TQ in rat liver mitochondrial membranes and the interference of TQ with the activity of mitochondrial and microsomal redox enzymes interacting with UQ. In view of the contradictory literature results regarding Toc, we determined the distribution of Toc, TQ, and UQ over inner and outer membranes of rat liver mitochondria. Irrespective of the preparation method, the TQ/Toc ratio tends to be higher in mitochondrial inner membranes than in outer membranes suggesting TQ formation by respiratory oxidative stress in vivo. The comparison of the catalytic activities using short-chain homologues of TQ and UQ showed decreasing selectivity in the order complex II (TQ activity not detected) > Qo site of complex III > Qi site of complex III > complex I ˜ cytochrome b5 reductase > cytochrome P-450 reductase (comparable reactivity of UQ and TQ). TQ binding to some enzymes is comparable to UQ despite low activities. These data show that TQ arising from excessive oxidative degradation of Toc can potentially interfere with mitochondrial electron transfer. On the other hand, both microsomal and mitochondrial enzymes contribute to the reduction of TQ to tocopheryl hydroquinone, which has been suggested to play an antioxidative role itself.

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