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Mitochondrial Cytochrome b560

  • Chang-An Yu
  • Linda Yu

Abstract

Cytochrome b 560 the succinate-ubiquinone (Q) reductase region of the mitochondrial electron transfer chain was first reported by Davis et al. (1,2). In spite of the detection of cytochrome b 560 in various succinate -Q1 reductase (3,4), and Complex II (5–7) preparations, this cytochrome has often been regarded as a contaminant of the denatured cytochromes from ubiquinol-cytochrome c reductase because it is not reducible by succinate, and the spectra of dithionite reduced cytochrome b 560 in these preparations resembles the spectra of a mixture of denatured cytochromes b and c 1 of ubiquinol-cytochrome c reductase. Thus, the importance of this particular cytochrome b 560 has been slighted in the mammalian system. The participation of cytochrome b 560 in succinate dehydrogenase (SDH) of Bacillus subtilis (8) and Neurospora crassa (9), however, is well recognized. Recently, a substrate reducible cytochrome ¿558 was detected in muscle mitochondrial succinate-Q reductase from Ascaris suum (10). In this paper we report the properties of mitochondrial cytochrome b560 and its possible function in succinate oxidation and fumarate reduction.

Keywords

Succinate Dehydrogenase Cytochrome B560 Midpoint Potential Succinate Oxidation Soret Absorption 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

DCIP

dichlorophenolindophenol

GMD

N-D-gluco-N-methyldecamide

Q

ubiquinone

Q2

2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone

QPs

a protein complex that converts SDH into succinate-Q reductase

SDH

succinate dehydrogenase

SDS

sodium dodecylsulfate

TTFA

2-thenoyltrifluoroacetone

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References

  1. 1.
    Davis, K. A., Hatefi, Y., Poff, K. L., and Butler, W. L. (1972) Biochem. Biophys. Res. Commun., 1984–1990.Google Scholar
  2. 2.
    Davis, K. A., Hatefi, Y., Poff, K. L., and Butler, W. L. (1973). Biochim. Biophys. Acta, 221, 341–356.Google Scholar
  3. 3.
    Yu, L., and Yu, C. A. (1982) J. Biol. Chem., 252, 2016–2021.Google Scholar
  4. 4.
    Tushurashvili, P. R., Gavrikova, E. V., Ledenev, A. N., and Vinogradov, A. D. (1985) Biochim. Biophys. Acta, 809, 145–159.CrossRefGoogle Scholar
  5. 5.
    Ziegler, D. M., and Doeg, K. A. (1962) Arch. Biochem. Biophys., 22, 41–50.CrossRefGoogle Scholar
  6. 6.
    Baginsky, M. L, and Hatefi, Y. (1969) J. Biol. Chem., 244, 5313–5319.Google Scholar
  7. 7.
    Hatefi, Y., and Stiggall, D. L. (1978) Methods in Enzymol, 52, 21–27.CrossRefGoogle Scholar
  8. 8.
    Hederstedt, L., Holmgren, E., and Rutberg, L. (1979) J. Bacteriol., 370–376.Google Scholar
  9. 9.
    Weiss, H., and Kolb, H. J. (1979) Eur. J. Biochem., 22, 139–149.CrossRefGoogle Scholar
  10. 10.
    Takamiya S., Furushima, R., and Oya, H. (1986) Biochim. Biophys. Acta, 848 99–107.CrossRefGoogle Scholar
  11. 11.
    Yu, C. A., Yu, L., and King, T. E. (1974) J. Biol. Chem., 242, 4905–4910.Google Scholar
  12. 12.
    Yu, C. A., and Yu, L. (1980) Biochemistry, 12, 5717–5720.Google Scholar
  13. 13.
    Ackrell, B. A. C., Bethany-Ball, M., and Kearney, E. B. (1980) J. Biol. Chem., 255, 2761–2769.Google Scholar
  14. 14.
    Hatefi, Y., and Galante, Y. M. (1980) J. Biol. Chem., 255, 5530–5537Google Scholar
  15. 15.
    Yu, L., Xu, J-X., Haley, P., and Yu,C. A. (1987) J. Biol. Chem., 262. 1137–1143.Google Scholar
  16. 16.
    Paul, K. G., Theorell, H., and Akeson, A. (1953) Acta Chem. Scand., 7 1284–1294.CrossRefGoogle Scholar
  17. 17.
    Macker, B. (1961) Biochim. Biophys. Acta 50, 141–146.CrossRefGoogle Scholar
  18. 18.
    Ohnishi, T., Salerno, J. C., Winter, D. B., Lim, J., Yu, C. A., Yu, L., and King, T. E. (1976) J. Biol. Chem., 251 2094–2104.Google Scholar
  19. 19.
    Salerno, J. C. (1984) J. Biol. Chem., 252, 2331–2336.Google Scholar
  20. 20.
    DeVries, S., and Albracht, S. P. J. (1979) Biochim. Biophys. Acta, 546, 334–340.CrossRefGoogle Scholar
  21. 21.
    Orme-Jonson, N. R., Hansen, R. E., and Beinert, H. (1974) J. Biol. Chem., 249. 1928–1939.Google Scholar
  22. 22.
    Yu, C. A., and Yu, L. (1981) Biochim. Biophys. Acta, 622, 383–386.Google Scholar
  23. 23.
    Ernster, L., and Lee, C. P. (1967) Methods Enzymol., 10 729–738.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Chang-An Yu
    • 1
  • Linda Yu
    • 1
  1. 1.Department of BiochemistryOklahoma State UniversityStillwaterUSA

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