Abstract
Although duroquinone had little effect upon NADH oxidation in neutral lipid depleted mitochondria, durohydroquinone was oxidized by ETP at a rate sensitive to antimycin A. Fractionation of mitochondria into purified enzyme systems showed durohydroquinone: cytochromec reductase to be concentrated in NADH: cytochromec reductase, absent in succinate:cytochromec reductase, and decreased in reduced coenzyme Q:cytochromec reductase. Durohydroquinone oxidation could be restored by recombining reduced coenzyme Q:cytochromec reductase with NADH:coenzyme Q reductase. Pentane extraction had no effect upon either durohydroquinone or reduced coenzyme Q10 oxidation, indicating lack of a quinone requirement between cytochromesb andc. Both chloroquine diphosphate and acetone (96%) treatment irreversibly inhibited NADH but not succinate oxidation. Neither reagents had any effect upon durohydroquinone oxidation but both inhibited reduced coenzyme Q10 oxidation 50%, indicating a site of action between Q10 and duroquinone sites. Loss of chloroquine sensitive reduced coenzyme Q10 oxidation after acetone extraction suggests two sites for Q10 before cytochromeb.
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Hare, J.F., Crane, F.L. A durohydroquinone oxidation site in the mitochondrial transport chain. J Bioenerg Biomembr 2, 317–326 (1971). https://doi.org/10.1007/BF01963828
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DOI: https://doi.org/10.1007/BF01963828