References
- Boveris A., Chance B. The cellular production of hydrogen peroxide. Biochem. J. 1973; 128: 617–630
- Loschen G., Azzi A., Flohé L. Mitochondrial H2O2 formation at site II. Hoppe Seyer' Z. Physiol. Chem. 1973; 354: 791–794
- Boveris A., Cadenas E. Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration. FEBS Lett. 1975; 54: 311–314
- Nohl H., Hegner D. Do mitochondria produce oxygen radicals in vivo?. Eur. J. Biochem. 1978; 82: 563–567
- Nohl H., Jordan W. The mitochondrial site of superoxide formation. Biochem. Biopliys. Res. Com. 1986; 138: 533–539
- Nohl H., Jordan W., Hegner D. Mitochondrial formation of hydroxyl radicals by an ubisemiquinone-dependent reaction. An alternative pathway of the iron-catalysed Haber-Weiss cycle. Hoppe Seyler' Z. Physiol. Chem. 1982; 363: 599–607
- Boveris A., Cadenas E., Stoppani A. O.M. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 1976; 156: 435–444
- Cadenas E., Boveris A., Ragan C. I., Stoppani A. O.M. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef heart mitochondria. Arch. Biochem Biophys. 1977; 180: 248–257
- Trumpower B. L., Simmons Z. Diminished inhibition of mitochondrial electron transfer from succinate to cytochrome c by thenoyltrifluoroacetone induced by antimycin. J. Biol. Chem. 1979; 254: 4608–4616
- de Vries S., Albracht S. P.J., Berden J. A., Marres C. A.M., Slater E. C. The effect of pH ubiquinone depletion and myxothiazol on the reduction kinetics of the prosthetic groups of ubiquinol: Cytochrome c. Biochim. Biophyx. Acta 1983; 723: 91–103
- Becker W. F., Jagow G. V., Thierbach G, Reichenbach H. The new antibiotic myxothiazol a valuable inhibitor at the second phosphorylation site. Hoppe Seyler's Z. Physiol. Chem. 1980; 361: 1467
- Trumpower L. B. New concepts on the role of ubiquinone in the mitochondrial respiratory chain. J. Bioenergetics, Biomem. 1981; 13: 1–24
- Maride D. L., Hodgson W. G. Reduction of oxygen to superoxide anion in aprotic solvents. Anal. Chem. 1965; 37: 1562–1565
- Wood P. M. The redox potential of the system oxygen-superoxide. FEBS Lett. 1974; 44: 22–24
- Jlan Y. A., Czapski G., Meisel D. The one-electron transfer redox potentials of free radicals. Biochim. Biophys. Acta 1976; 430: 209–224
- Lenaz G., Esposti D., Fahmy T., Fato R., Rugolo M., Parenti Castelli G. Localization and Function of Coenzyme Q in the inner mitochondrial membrane. Biomedical and Clinical Aspects of Coenzyme Q, K. Folkers, Y. Yamamura. Elsevier, Amsterdam 1984; 33–42
- Wikström M. K.F., Berden J. A. Oxidoreduction of cytochrome b in the presence of antimycin. Biochim. Biophys. Acta 1972; 283: 403–420
- Loschen G., Azzi A., Flohé L. Mitochondrial H2O2 formation: relationship with energy conservation. FEBS Lett. 1973; 33: 84–88
- Nohl H., de Silva D., Summer K. H. 2.3,7,8 Tetrachlorodibenzo-p-dioxin induces oxygen activation associated with cell respiration. Free Rad. Biol. Med. 1989; 6: 369–374
- Turrens J. F., Alexandre A., Lehninger A. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem. Biophys. 1985; 237: 408–414
- Nohl H., Jordan W. The involvernent of biological quinones in the formation of hydroxyl radicals via the Haber-Weiss reaction. Bioorganic Chem. 1987; 15: 374–382