Summary
Superoxide dismutase, catalase and methional proved capable of inhibiting the microsomal oxidation of thiobenzamide, which is most probably catalyzed by the flavin-containing monooxygenase. This indicates that excited oxygen species (e. g.·O −2 , H2O2, ·OH) are involved in the catalytic cycle of this enzymatic reaction. CO, which inhibits the cytochrome P-450-dependent oxygen radical formation, had no effect on the oxidation reaction, suggesting that the source of the reactive oxygen species is not the microsomal mixed-function oxidase.
References
Poulsen, L. L., and Ziegler, D. M., J. biol. Chem.254 (1979) 6449.
Ziegler, D. M. in: Enzymatic Basis of Detoxication, vol. 1, p. 201. Ed. W. B. Jakoby, Academic Press, New York 1980.
Paine, A. J., Biochem. Pharmac.27 (1978) 1805.
Breeman, B. A., and Crapo, J. D., Lab. Invest.47 (1982) 412.
Johansson, I., and Ingelman-Sundberg, M., J. biol. Chem.258 (1983) 7311.
Younes, M., and Weser, U., Biochim. biophys. Acta526 (1978) 644.
Remmer, H., Greim, H., Schenkman, J. B., and Estabrook, R. W., Methods Enzymol.10 (1967) 703.
Cashman, J. R., and Hanzlik, R. P., Biochem. biophys. Res. Commun.98 (1981) 147.
Wilson, R. L., Ciba Fd Symp.65 (1979) 19.
Afanasev, I. B., Kuprianova, N. S., and Letuchaia, A. V., in: Oxygen Radicals in Chemistry and Biology, p. 17. Eds W. Bors, M. Saran and D. Tait. Walter de Gruyter, Berlin and New York 1984.
Pryor, W. A., and Tang, R. H., Biochem. biophys. Res. Commun.81 (1978) 498.
Younes, M., Albrecht, M., and Siegers, C.-P. Res. Commun. chem. Path. Pharmac.40 (1983)121.
Kuthan, H., and Ullrich, V., Eur. J. Biochem.126 (1982) 583.
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Younes, M. Involvement of reactive oxygen species in the microsomal S-oxidation of thiobenzamide. Experientia 41, 479–481 (1985). https://doi.org/10.1007/BF01966157
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DOI: https://doi.org/10.1007/BF01966157