ubiquinol and fumaric-acid

O2- generation in mitochondrial electron transport systems, especially the NADPH-coenzyme Q10 oxidoreductase system, was examined using a model system, NADPH-coenzyme Q1-NADPH-dependent cytochrome P-450 reductase. One electron reduction of coenzyme Q1 produces coenzyme Q1-. and O2- during enzyme-catalyzed reduction and O2+ coenzyme Q1-. are in equilibrium with O2- + coenzyme Q1 in the presence of enough O2. The coenzyme Q1-. produced can be completely eliminated by superoxide dismutase, identical to bound coenzyme Q10 radical produced in a succinate/fumarate couple-KCN-submitochondrial system in the presence of O2. Superoxide dismutase promotes electron transfer from reduced enzyme to coenzyme Q1 by the rapid dismutation of O2- generated, thereby preventing the reduction of coenzyme Q1 by O2-. The enzymatic reduction of coenzyme Q1 to coenzyme Q1H2 via coenzyme Q1-. is smoothly achieved under anaerobic conditions. The rate of coenzyme Q1H2 autoxidation is extremely slow, i.e., second-order constant for [O2][coenzyme Q1H2] = 1.5 M-1.s-1 at 258 microM O2, pH 7.5 and 25 degrees C.

Topics: Anaerobiosis; Animals; Cattle; Electron Spin Resonance Spectroscopy; Electron Transport; Free Radicals; Fumarates; Hydrogen-Ion Concentration; Kinetics; Mitochondria; Mitochondria, Heart; Models, Biological; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen Consumption; Potassium Cyanide; Submitochondrial Particles; Succinates; Succinic Acid; Superoxide Dismutase; Superoxides; Ubiquinone; Vitamin K