Iron and Copper Proteins pp 161-181 | Cite as
Factors Controlling the Turnover Number of Succinate Dehydrogenase: A New Look at an Old Problem
Chapter
Abstract
Identification of the rate-limiting step in the catalytic cycle of succinate dehydrogenase and the related problem of defining the factors which determine its turnover number have for a long time occupied the interest of many investigators. During the past two years a collaboration among several laboratories has been initiated in order to use a variety of experimental approaches to these problems. The present report summarizes the progress which has been achieved.
Keywords
Succinate Dehydrogenase Soluble Enzyme Turnover Number Succinate Dehydrogenase Activity Membrane Environment
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References
- 1.Singer, T. P. (1974) Methods of Biochemical Analysis 22, 123–175.PubMedCrossRefGoogle Scholar
- 2.Singer, T.P. , and Cremona, T. (1964) in Oxygen in the Animal Organism (Dickens, F. and Neil, E. , eds), pp 179–214, Pergamon Press, Oxford.Google Scholar
- 3.Beinert, H. , Ackrell, B.A.C., Kearney, E.B. , and Singer, T.P. (1975) Eur. J. Biochem. 54, 185–194.PubMedCrossRefGoogle Scholar
- 4.Vinogradov, A.D., Gavrikova, E.V., and Goloveshkina, V.G. (1975) Biochem. Biophys. Res. Communs. 65, 1264–1269.CrossRefGoogle Scholar
- 5.Vinogradov, A.D., Ackrell, B.A.C, and Singer, T.P. (1975) Biochem. Biophys. Res. Commun. 67, 803–809.PubMedCrossRefGoogle Scholar
- 6.Singer, T.P. (1966) in Comprehensive Biochemistry, Vol. 14 (Florkin, M., and Stotz, E.H., eds.) pp 127–198, Elsevier Publishing Co. Amsterdam.Google Scholar
- 7.Davis, K.A. and Hatefi, Y. (1971) Biochemistry 10, 2509–2516.PubMedCrossRefGoogle Scholar
- 8.Rossi, E., Norling, B. , Persson, B. and Ernster, L. (1970) Eur. J. Biochem. l6, 508–513.CrossRefGoogle Scholar
- 9.Singer, T.P., Kearney, E.B., and Kenney, W.C. (1973) Advan. Enzymol. 37, 189–272.Google Scholar
- 10.Giuditta, A., and Singer, T.P. (1959) J. Biol. Chem. 234, 661–671.Google Scholar
- 11.Ziegler, D.M. (1961) in Biological Structure and Function, Vol. II. (Goodwin, T.W. and Lindberg, O.) pp 253–264, Academic Press, New York.Google Scholar
- 12.White, G.A. (1971) Biochem. Biophys. Res. Commun. 44, 1212–1219.PubMedCrossRefGoogle Scholar
- 13.Singer, T.P. , Beinert, H. , Ackrell, B.A.C, and Kearney, E.B. (1975) in Proceedings of the Tenth FEBS Meeting, Paris (Raoul, Y., ed) pp 173–185, ASP, .Amsterdam.Google Scholar
- 14.Ohnishi, T., Winter, D.B. , Lim, J., and King, T.E. (1974) Biochem. Biophys. Res. Commun. 6l, 1017–1025.CrossRefGoogle Scholar
- 15.Ohnishi, T., Leigh, J.S. , Winter, D.B., Lim, J., and King, T.E. (1974) Biochem. Biophys. Res. Commun. 61, 1026–1035.CrossRefGoogle Scholar
- 16.Coles, C.J., Tisdale, H.D. , Kenney, W.C., and Singer, T.P. (1972) Physiol. Chem. Phys. 4, 301–316.PubMedGoogle Scholar
- 17.King, T.E. (1967) Methods Enzymol. 10, 322–331.CrossRefGoogle Scholar
- 18.Baginsky, M.L. and Hatefi, Y. (1968) Biochem. Biophys. Res. Commun. 32, 945–950.PubMedCrossRefGoogle Scholar
- 19.King, T.E., Winter, D., and Steele, W. (1972) in Structure and Function of Oxidation-Reduction Enzymes (Akeson, A., and Ehrenberg, A.,eds) pp 519–532, Pergamon Press, Oxford.Google Scholar
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© Plenum Press, New York 1976