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Inhibition of membrane-bound succinate dehydrogenase by disulfiram

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Abstract

The effect of disulfiram on succinate oxidase and succinate dehydrogenase activities of beef heart submitochondrial particles was studied. Results show that disulfiram inhibits both functions. Succinate and malonate suppress the inhibitory action of disulfiram when succinate dehydrogenase is stabilized in an active conformation. Disulfiram is not able to inhibit the enzyme when succinate dehydrogenase is inactivated by oxaloacetate. The inhibitory effect of disulfiram is reverted by the addition of dithiothreitol. From these results, it is proposed that disulfiram inhibits the utilization of succinate by a direct modification of an -SH group located in the catalytically active site of succinate dehydrogenase.

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References

  • Ackrell, A. C. B., Kearney, B. E., and Singer, T. P. (1978).Methods Enzymol. 53, 466–483.

    Google Scholar 

  • Chávez, E., Bravo, C., and Jay, D. (1986).J. Bioenerg. Biomembr. 18, 93–99.

    Google Scholar 

  • Chávez, E., Zazueta, C., and Bravo, C. (1989).J. Bioenerg. Biomembr. 21, 335–345.

    Google Scholar 

  • Coles, C. J., and Singer, T. P. (1977).FEBS Lett. 82, 267–268.

    Google Scholar 

  • Eneanya, D. I., Bianchine, J. R., Duran, D. O., and Andersen, B. D. (1981).Annu. Rev. Pharmacol. Toxicol. 21, 575–596.

    Google Scholar 

  • Feinman, L., and Lieber, C. S. (1974). Liver disease in alcoholism. InThe Biology of Alcoholism. Vol. 3,Clinical Pathology. (Kissin, B., and Begleiter, H., eds.), Plenum Press, New York, pp. 303–338.

    Google Scholar 

  • Goldstein, M., Mussacchio, J., Kopin, I., and Axelrod, J. (1964).Life Sci. 3, 763–767.

    Google Scholar 

  • Graham, W. D. (1951).J. Pharm. Pharmacol. 3, 160–164.

    Google Scholar 

  • Gutman, M. (1977).Biochemistry 16, 3067–3072.

    Google Scholar 

  • Gutman, M. (1978).Mol. Cell. Biochem. 20, 41–60.

    Google Scholar 

  • Gutman, M., Kearney, E. B., and Singer, T. P. (1971).Biochemistry 10, 2726–2733.

    Google Scholar 

  • Hassinen, I. (1966).Biochem. Pharmacol. 15, 1147–1153.

    Google Scholar 

  • Jurkovitz, M., Scott, K. M., Altschuld, R., Merola, A. J., and Brierley, G. P. (1974).Arch. Biochem. Biophys. 165, 98–113.

    Google Scholar 

  • Kearney, E. B. (1957).J. Biol. Chem. 229, 363–375.

    Google Scholar 

  • Kearney, E. B., Ackrell, B. A. C., Mayer, M., and Singer, T. P. (1974).J. Biol. Chem. 249, 2016–2020.

    Google Scholar 

  • Kelner, M. J., and Alexander, N. M. (1986).J. Biol. Chem. 261, 1636–1641.

    Google Scholar 

  • Kenney, W. C. (1975).J. Biol. Chem. 250, 3089–3094.

    Google Scholar 

  • Kotlyar, A. B., and Vinogradov, A. D. (1984).Biochim. Biophys. Acta 784, 24–34.

    Google Scholar 

  • Lee, C. P., and Ernster, L. (1966). InSymposium on the Regulation of Metabolic Processes in Mitochondria (Tage, J. M., Papa, S., Quagliariello, E., and Slater, E. C., eds.), Vol. 7, Elsevier North-Holland, New York, pp. 218–234.

    Google Scholar 

  • Le-Quôc, K., Le-Quôd, D., and Gaudemer, Y. (1981).Biochemistry 20, 1705–1710.

    Google Scholar 

  • Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. (1951).J. Biol. Chem. 193, 265–275.

    Google Scholar 

  • Mowery, P. C., Steekamp, D. J., Ackrell, B. A. C., Singer, T. P., and White, G. A. (1977).Arch. Biochem. Biophys. 178, 495–506.

    Google Scholar 

  • Richert, D., Vanderlinde, R., and Westerfeld, W. (1950).J. Biol. Chem. 183, 261–274.

    Google Scholar 

  • Singer, T. P., Kearney, B. E., and Kenney, C. W. (1973).Adv. Enzymol. 5, 189–271.

    Google Scholar 

  • Vinogradov, A. D., Zimakova, N. I., and Solntseva, T. I. (1971).Dokl. Akad. Nauk. USSR 201, 359–362.

    Google Scholar 

  • Vinogradov, A. D., Winter, D. W., and King, T. E. (1972).Biochem. Biophys. Res. Commun. 49, 441–444.

    Google Scholar 

  • Vinogradov, A. D., Gavrikova, E. V., and Zuevsky, V. V. (1976).Eur. J. Biochem. 63, 365–371.

    Google Scholar 

  • Whereat, A. F., Hull, F. E., Orishimo, M. W., and Rabinowitz, J. (1967).J. Biol. Chem. 242, 4013–4022.

    Google Scholar 

  • Wojtczak, L., Wojtczak, A. B., and Ernster, L. (1969).Biochim. Biophys. Acta 191, 10–21.

    Google Scholar 

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Jay, D. Inhibition of membrane-bound succinate dehydrogenase by disulfiram. J Bioenerg Biomembr 23, 335–343 (1991). https://doi.org/10.1007/BF00762226

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  • DOI: https://doi.org/10.1007/BF00762226

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