Journal of Bioenergetics and Biomembranes

, Volume 26, Issue 6, pp 619–626 | Cite as

Composition and function of cytochrome b559 in reaction centers of photosystem II of green plants

  • Vladimir A. Shuvalov


A review of a recent study of the spectral and thermodynamic properties of cytochrome b559 as well as of the electron transfer between b559 and photosystem II reaction center cofactors in isolated D1/D2/cytochrome b559 complex RC-2 is presented. Attention is paid to the existence of intermediary-potential (IP, +150 mV) and extra-low-potential (XLP, −45 mV) hemes located close to the acceptor (quinone) and donor (P680) sides of the reaction center cofactors, respectively. These hemes found in isolated RC-2 probably correspond to the high-potential and low-potential hemes in chloroplasts, respectively. The above location of the hemes is believed to allow the photoreduction of the XLP heme and photooxidation of the IP heme. The electron transfer between the two hemes is discussed in terms of the cyclic electron flow and possible involvement in water splitting.

Key words

Cytochrome b559 D1D2 Cyt b559 complex electron transfer Photosystem II 


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  1. Babcock, G. T., Widger, W. R., Cramer, W. A., Oertling, W. A., and Metz, J. G. (1985).Biochemistry 24 3638–3645.PubMedGoogle Scholar
  2. Barber, J., and de Las Rivas, J. (1993).Proc. Natl. Acad. Sci. USA 90 10942–10946.PubMedGoogle Scholar
  3. Blumberg, W. E., and Peisach, J. (1971). InProbes of Structure and Function of Macromolecules and Membranes (Chance, B., Yonetani, T., and Mildvan, A. S., eds.), Academic Press, New York, Vol. 2, pp. 215–228.Google Scholar
  4. Buser, C. A., Diner, B. A., and Brudvig, G. M. (1992).Biochemistry 31 11441–11459.PubMedGoogle Scholar
  5. Chapman, D. J., Gounaris, K., and Barber, J. (1988).Biochim. Biophys. Acta 933 423–431.Google Scholar
  6. Cox, R. P., and Bendall, D. S. (1972).Biochim. Biophys. Acta 283 124–135.PubMedGoogle Scholar
  7. Cramer, W. A., and Butler, W. L. (1967).Biochim. Biophys. Acta 143 332–339.PubMedGoogle Scholar
  8. Cramer, W. A., and Whitmarsh, J. (1977).Annu. Rev. Plant Physiol. 28 133–172.Google Scholar
  9. Cramer, W. A., Theg, S. M., and Widger, W. R. (1986).Photosynth. Res. 10 393–403.Google Scholar
  10. Debus, R. J. (1992).Biochim. Biophys. Acta 1102 269–352.PubMedGoogle Scholar
  11. Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. (1985).Nature (London)318 618–624.Google Scholar
  12. Erixon, K., Lozier, R., and Butler, W. L. (1972).Biochim. Biophys. Acta 267 375–382.PubMedGoogle Scholar
  13. Fujita, I., Davies, M. S., and Fajer, J. (1978).J. Am. Chem. Soc. 100 6280–6282.Google Scholar
  14. Gounaris, K., Chapman, D. J., and Barber, J. (1988).FEBS Lett. 240 143–147.Google Scholar
  15. Heber, U., Kirk, M. R., and Boardman, N. K. (1979).Biochim. Biophys. Acta 546 292–306.PubMedGoogle Scholar
  16. Horton, P., Whitmarsh, J., and Cramer, W. A. (1976).Arch. Biochem. Biophys. 176 519–524.PubMedGoogle Scholar
  17. Kaminskaya, O. P., and Shuvalov, V. A. (1994).FEBS Lett., submitted.Google Scholar
  18. van Kan, P. J. M., Otte, S. C. M., Kleinherenbrik, F. A. M., Nieveen, M. C., Aartsma, T. J., and van Gorkom, H. J. (1990).Biochim. Biophys. Acta 1020 146–152.Google Scholar
  19. Matsuda, H., and Butler, W. L. (1983).Biochim. Biophys. Acta 724 123–127.Google Scholar
  20. Michel, H., and Deisenhofer, J. (1988).Biochemistry 27 1–7.Google Scholar
  21. Nanba, O., and Satoh, K. (1987).Proc. Natl. Acad. Sci. USA 84 109–112.Google Scholar
  22. Parkasi, H. B., and Wermaas, W. F. J. (1992). InThe Photosystems: Structure, Function and Molecular Biology (Barber, J., ed.), Elsevier, Amsterdam, pp. 231–257.Google Scholar
  23. Satoh, K., Hansson, O., and Mathis, P. (1970).Biochim. Biophys. Acta 1016 121–126.Google Scholar
  24. Schonbaum, G. R., and Chance, B. (1976). InThe Enzymes (Boyer, P. D., ed.), Vol. 13, Part C, pp. 363–408.Google Scholar
  25. Shuvalov, V. A., and Kaminskaya, O. P. (1993). In Abstracts of Topical ESF workshop “Spectroscopy of isolated D1D2 reaction centers,” p. 1, Max-Planck-Inst. fur Strahlenchemie, Mulheim.Google Scholar
  26. Shuvalov, V. A., Heber, U., and Schreiber, U. (1989).FEBS Lett. 258 27–31.Google Scholar
  27. Shuvalov, V. A., Schreiber, U., and Heber, U. (1994a).FEBS Lett. 337 226–230.PubMedGoogle Scholar
  28. Shuvalov, V. A., Fiege, R., Schreiber, U., Lendzian, F., and Lubitz, W. (1994b).Biochim. Biophys. Acta, to be submitted.Google Scholar
  29. Takahashi, Y., Hansson, O., Mathis, P., and Satoh, K. (1987).Biochim. Biophys. Acta 893 49–59.Google Scholar
  30. Vallon, O., Tae, G.-S., Cramer, W. A., Simpson, D., Hoyer-Hansen, G., and Bogorad, L. (1989).Biochim. Biophys. Acta 975 132–141.PubMedGoogle Scholar
  31. Widger, W. R., Cramer, W. A., Hermodson, M., and Herrmann, R. G. (1985).FEBS Lett. 191 186–190.Google Scholar

Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • Vladimir A. Shuvalov
    • 1
  1. 1.Belozersky Institute of Physical Chemical BiologyMoscow State UniversityMoscowRussia

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