Abstract
Since the discovery of succinate dehydrogenase, this enzyme has remained as one of the, if not the, most colorful enzymes essential for mitochondrial electron transport. Perhaps because it is tenaciously attached to the membrane and “uniquely” reacts with electron acceptors, reports on the serious attempts of its solubilization did not appear until 1955. It is true that Tsou in 1950 definitively established the non-identity of succinate dehydrogenase and cytochrome b in the respiratory chain (1); this establishment dispersed and clarified a major confusion which otherwise might have hindered progress further. Nonetheless, even today the structure-function relationship of succinate dehydrogenase is still largely unknown. This paper will briefly review our work on a specific facet of the dehydrogenase, i. e. the iron-sulfur centers by biochemical and EPR studies.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Tsou, C.L. (1951) Biochem. J. 49, 512–520.
Kearney, E.B., and Singer, T. P. (1956) J. Biol. Chem. 219, 963.
Dickens, F., and McIlwain, H. (1938) Biochem. J. 32, 1615.
Dickens, F. (1936) Biochem. J. 30, 1064 and 1233.
McIlwain, H. (1937) J. Chem. Soc. 1704.
Singer, T. P., Kearney, E. B., and Bernath, P. (1956) J. Biol. Chem. 223, 599–613.
Wang, T. Y. , Tsou, C. L. , and Wang, Y. L. (1956) Sci. Sinica 5, 73–85.
Chi, T. F., Wang, Y. L., Tsou, C. L., Fang, Y. C., and Yu, C. H. (1965) Sci. Sinica 14, 1193–1204 and papers cited.
Massey, V. (1957) J. Biol. Chem. 229, 763–770.
Yasunobu, K. T., and Tanaka, M. (1973) in Iron-Sulfur Proteins (W. Lovenberg, ed.) Vol. 2, pp. 29–130, Academic Press, New York.
Personal communications with Green, D.E.; see also, for example, Mackler, B., Repaske, R., Kohout, P.M., and Green, D. E. (1954) Biochim. Biophys. Acta 15, 437–458.
Mackler, B., and Green D. E. (1956) Biochim. Biophys. Acta 21, 1–6.
Crane, F. L., Glenn, J. L., and Green, D. E. (1956) Biochim. Biophys. Acta 22, 475–487.
Mackler, B., Mahler, H. R., and Green, D. E. (1954) J. Biol. Chem. 210, 149–164.
Mahler, H. R., and Elowe, D. G. (1953) J. Am. Chem. Soc. 75, 5769–5770.
Mahler, H. R., and Elowe, D. G. (1954) J. Biol. Chem. 210, 165–179.
Beinert, H., and Sands, R. H. (1959) Biochem. Biophys. Res. Commun. 1, 171–174.
Sands, R. H. , and Beinert, H. (1959) Biochem. Biophys. Res. Commun. 1, 175–178.
Discussions, Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.) (1965), especially Vol. 1, pp. 374–380 and 399–417, John Wiley and Sons, New York, New York.
Tsou, C. L., and Wu, C. Y. (1956) Sci. Sinica 5, 263–270.
Dixon, M., and Webb, E. C. (1958) Enzymes, Longmans, Green, London.
Smith, L., and Stotz, E. (1954) J. Biol. Chem. 209, 819–828.
Keilin, D., and Hartree, E. F. (1940) Proc. Roy. Soc. B129, 277–306
King, T. E. (1966) in Advances in Enzymology (F.F. Nord, ed.) Vol. 28, pp. 155–236, John Wiley and Sons, New York, New York.
Yu, C. A., Yu, L., and King, T. E. (1974) J. Biol. Chem. 249, 4905–4910.
Olcott, H. S., and Franckel-Conrat, H. (1947) Chem. Rev. 41, 151–197.
Mauthner, J. (1912) Z. Physiol. Chem. Hoppe-Seyl. 78, 28–36.
Hopkins, F. G., and Morgan, E. J. (1938) Biochem. J. 32, 611–620.
Hopkins, F. G., Morgan, E. J., and Lutwok-Mann, C. (1938) Biochem. J. 32, 1829–1848.
Keilin, D., and King, T. E. (1958) Nature, 181, 1520–1522.
King, T. E. (1962) Biochim. Biophys. Acta 59, 492–494.
Beinert, H., and Lee, W. (1961) Biochem. Biophys. Res. Commun. 5, 40–45.
King, T. E., Howard, R. L., and Mason, H. S. (1961) Biochem. Biophys. Res. Commun. 5, 329–333.
Commoner, B., and Hollacher, T. C. (1960) Proc. Nat. Acad. Sci. U.S.A. 46, 405–411.
King, T. E. (1965) in Non-Heme Iron Proteins: Role in Energy Conversion (A. San Pietro, ed.) pp. 413–419, Antioch Press, Yellow Springs, Ohio.
King, T. E. (1965) in Flavins and Flavoproteins (E. C. Slater, ed.), Discussion pp. 200–203, Elsevier, Amsterdam.
Wilson, D. F., and King, T. E. (1967) Biochim. Biophys. Acta 131, 265–279.
DerVartanian, D. V. (1966) in Flavins and Flavoproteins (E. C. Slater, ed.) Discussion, p. 203, Elsevier, Amsterdam.
Colpa, J. P. (1966) in Flavins and Flavoproteins (E. C. Slater, ed.) Discussion, p. 203, Elsevier, Amsterdam.
King, T. E. (1964) Biochem. Biophys. Res. Commun. 16, 511–515.
Zeylemaker, W. P., DerVartanian, D., and Veeger, C. (1965) Biochim. Biophys. Acta 99, 183–184.
King, T. E., and Morris, R. O. (1967) Methods Enzymol. 10, 634–641.
King, T. E., Winter, D., and Steele, W. (1972) in Oxidation Reduction Enzymes (A. Akeson and A. Ehrenberg, eds.) pp. 519–532, Pergamon Press, Oxford and New York.
Davis, K. A., and Hatefi, Y. (1971) Biochemistry 10, 2509–2516.
Righetti, O. O., and Cerletti, O. O. (1971) FEBS Lett. 13, 181–185.
Coles, C. J., Tisdale, H. D., Kenny, W. C., and Singer, T. P. (1972) Physiol. Chem. Phys. 4, 301–316.
Beinert, H. (1973) in Iron-Sulfur Proteins (W. Lovenberg, ed.) Vol. 1, Chapter 1, Academic Press, New York.
Ohnishi, T., Winter, D. B., Lim, J., and King, T. E. (1973) Biochem. Biophys. Res. Commun. 53, 231–237.
Ohnishi, T., Leigh, J. S., Winter, D. B., Lim, J., and King, T. E. (1974) Biochem. Biophys. Res. Commun. 61, 1026–1035.
Ohnishi, T., Salerno, J. C., Winter, D. B., Lim, J., Yu, C. A., Yu, L., and King, T. E. (in preparation).
Beinert, H., and Ruzicka, J. (1975) in Abstracts of International Symposium on Electron Transfer Chains and Oxidative Phosphorylation, Fasano, September 15–18, p. 7.
Beinert, H., Ackrell, B. A. C., Kearney, E. B., and Singer, T. P. (1975) Eur. J. Biochem. 54, 185–194.
Bartsch, R. G. (1963) in Bacterial Photosynthesis (H. Gest, A. San Pietro, and L. P. Vernon, eds.) pp. 315–326, Antioch Press, Yello Spring, Ohio.
Green, D. E., Wharton, D. C., Tzagoloff, A., Rieske, J. S. and Brierley, G. P. (1965) in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.) Vol. 2, pp. 1032–1076, John Wiley and Sons, New York, New York.
Ohnishi, T., Winter, D. B., Lim, J., and King, T. E. (1974) Biochem. Biophys. Res. Commun. 61, 1017–1025.
Ohnishi, T., Lim, J., Winter, D. B., and King, T. E. (in preparation).
Ohnishi, T., Winter, D. B., and King, T. E. (1976) Proc. of International Symposium on Electron Transfer Chains and Oxidative Phosphorylation, Fasano, September 15–18, p. 7
King, T. E. (1963) J. Biol. Chem. 238, 4037–4051.
Ketterman, Jr., J. (1964) Dissertation, Oregon State University, Corvallis, Oregon.
Vinogradov, A. D., Gavrikova, E. V., and Goloveshkiva, V. G. (1975) FEBS Abstract No. 1265.
Lim, J., Yu, C. A., Vinogradov, A. D., Ketterman, Jr., J., and King, T. E. (in preparation).
King, T. E. (1963) J. Biol. Chem. 238, 4032–4036.
Orme-Johnson, N. R., Hansen, R. E., and Beinert, H. (1974) J. Biol. Chem. 249, 1928–1939.
Ackrell, B. A. C., Kearney, E. B., and Edmonason, D. (1975) J. Biol. Chem. 250, 7114–7119.
Ohnishi, T. (1975) Biochim. Biophys. Acta 387, 475–490.
Ohnishi, T., Cartledge, T. G., and Lloyd, D. (1975) FEBS Lett. 52, 90–94.
Leigh, J. S. (1970) J. Chem. Phys. 52, 2608–2612.
Mathews, R. , Charlton, S. , Sands, R. H. , and Palmer, G. (1974) J. Biol. Chem. 249, 4326–4328.
Keilin, D. , and King, T. E. (1958) Biochem. J. 69, 32p.
Giuditta, A., and Singer, T. P. (1959) J. Biol. Chem. 234, 666–671.
Keilin, D., and King, T. E. (1960) Proc. Roy. Soc. , London B152, 163–187.
Lee, C. P., and King, T. E. (1962) Biochim. Biophys. Acta 59, 716–718.
Winter, D. B., Ohnishi, T., and Wu, J. T. Y. (in preparation)
Wang, T. Y. , and Wang, Y. L. (1964) Sci. Sinica 13, 1779–1809.
Wu, J. T. Y. (1967) Dissertation, Oregon State University, Corvallis, Oregon.
DerVartanian, D. V. (1965) Dissertation, University of Amsterdam, The Netherlands.
DerVartanian, D. V., and Veeger, C. (1964) Biochim. Biophys. Acta 92, 233–247.
Takemori, S., and King, T. E. (1964) Science 144, 852–853.
Takemori, S., and King, T. E. (1964) J. Biol. Chem. 239, 3546–3558.
King, T. E., and Takemori, S. (1964) J. Biol. Chem. 239, 3559–3569.
Ford-Smith, M. H. (1964) The Chemistry of Complex Cyanide, Her Majesty’s Stationery Office, London.
Petering, D., Fee, J. A., and Palmer, G. (1971) J. Biol. Chem. 246, 643–653.
Wallace, E. F., and Rabinowitz, J. C. (1971) Arch. Biochem. Biophys. 146, 400–409.
Hylin, J. W., and Wood, J. L. (1959) J. Biol. Chem. 234, 2141–2144.
Sieker, L. C., Adams, E., and Jensen, L. H. (1972) Nature 235, 40–45.
Carter, C. W., Kraut, J., Freer, S. T., Alden, R. A., Sieker, L. C., Adman, E., and Jensen, L. H. (1972) Proc. Natl Acad. Sci. 69, 3526–3532.
Kearney, E. B., Ackrell, B. A. C., and Mayr, M. (1972) Biochem. Biophys. Res. Commun. 49, 1115–1121.
Winter, D. B., and King, T. E. (1974) Biochem. Biophys. Res. Commun. 56, 290–295.
Hanstein, W. G., Davis, K. A., Ghalambor, M. A., Hatefi, Y. (1971) Biochemistry 10, 2517.
Vinogradov, A. D., Winter, D. B., and King, T. E. (1972) Biochem. Biophys. Res. Commun. 49, 441–444.
Winter, D. B., and King, T. E. (1974) Biochem. Biophys. Res. Commun. 56, 290–295.
Kimura, T. (1971) J. Biol. Chem. 246, 5140.
Coucouvanis, D., and Lippard, S. J. (1968) J. Amer. Chem. Soc. 90, 3281.
Watenpaugh, K. D., Sieker, L. C., Herriott, J. K., and Jensen, L. H. (1971) Cold Spring Harbor Symp. Quant. Biol. 36, 359–367.
Brintzinger, H., Palmer, G., and Sands, R. H. (1966) Proc. Natl Acad. Sci. 55, 397.
Jensen, L. H. (1972) Abstr. Metalloenzyme Conf., Oxford, p. 5
Carter, Jr., C. W., Freer, S. T., Xuong, N. H., Alden, R. A., and Kraut, J. (1971) Cold Spring Harbor Symp. Quant. Biol. 36, 381–385.
Orme-Johnson, W. H. (1973) Ann. Rev. Biochem. 42, 159.
Piesach, J., Blumberg, W. E., Lode, E. T., and Coon, M. J. (1971) J. Biol. Chem. 246, 5877.
Orme-Johnson, W. H., and Sands, R. H. (1973) in The ïron-Sulfur Proteins (Lovenberg, W., ed.) p, 195, Academic Press, New York, New York.
Sweeney, W. V., Bearden, A. J., and Rabinowitz, J. C. (1974) Biochem. Biophys. Res. Commun. 59, 188–194.
Bruni, A., and Racker, E. (1968) J. Biol. Chem., 243, 962–971.
Schatz, G., and Saltzaber, J. (1971) in Probes of Structure and Function of Macromolecules and Membranes (Chance, B., Yonetani, T., and Mildvan, A. S., eds.) Vol. 1, 437–444, Academic Press, New York, New York.
Mitchell, P., FEBS Lett. (1975) 56, 1–6.
Singer, J. S., and Nicolson, G. L. (1972) Science 175, 720–732.
King, T. E., Yu, C. A., and Yu, L. (1976) in Electron-Transfer Chains and Oxidative Phosphorylation (Quagliariello, E., Palmieri, F., Papa, S., Siliprandi, N., and Slater, E. C., eds) pp. 105–118, North-Holland Publishing Co., Amsterdam.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1976 Plenum Press, New York
About this chapter
Cite this chapter
King, T.E., Ohnishi, T., Winter, D.B., Wu, J.T. (1976). Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase. In: Yasunodu, K.T., Mower, H.F., Hayaishi, O. (eds) Iron and Copper Proteins. Advances in Experimental Medicine and Biology, vol 74. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3270-1_15
Download citation
DOI: https://doi.org/10.1007/978-1-4684-3270-1_15
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-3272-5
Online ISBN: 978-1-4684-3270-1
eBook Packages: Springer Book Archive