Skip to main content
Log in

Comparative Study of Effects of Artificial Electron Donors on the AT-Band of Photosystem II Thermoluminescence

  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

Extraction of the Mn-cluster from photosystem II (PS II) inhibits the main bands of thermoluminescence and induces a new AT-band at –20°C. This band is attributed to the charge recombination between acceptor QA and a redoxactive histidine residue on the donor side of PS II. The effect of Mn(II) and Fe(II) cations as well as the artificial donors diphenylcarbazide and hydroxylamine on the AT-band of thermoluminescence was studied to elucidate the role of the redoxactive His residue in binding to the Mn(II) and Fe(II). At the Mn/PS II reaction center (RC) ratio of 90 : 1 and Fe/PS II RC ratio of 120 : 1, treatment with Mn(II) and Fe(II) causes only 60% inhibition of the AT-band. Preliminary exposure of Mn-depleted PS II preparations to light in the presence of Mn(II) and Fe(II) causes binding of the cations to the high-affinity Mn-binding site, thereby inhibiting oxidation of the His residue involved in the AT -band formation. The efficiency of the AT-band quenching induced by diphenylcarbazide and hydroxylamine is almost an order of magnitude higher than the quenching efficiency of Mn(II) and Fe(II). Our results suggest that the redox-active His is not a ligand of the high-affinity site and does not participate in the electron transport from Mn(II) and Fe(II) to YZ . The concentration dependences of the AT-band inhibition by Mn(II) and Fe(II) coincide with each other, thereby implying specific interaction of Fe(II) with the donor side of PS II.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

REFERENCES

  1. Nugent, J. H. A. (1996) Eur. J. Biochem., 237, 519–531.

    Google Scholar 

  2. Renger, G. (1997) Physiol. Plant., 100, 828–841.

    Google Scholar 

  3. Hankamer, B., and Barber, J. (1997) Annu. Rev. Plant Physiol. Plant Mol. Biol., 8, 641–671.

    Google Scholar 

  4. Kok, B., Forbush, B., and McGloin, M. (1970) Photochem. Photobiol., 11, 457–475.

    Google Scholar 

  5. Tamura, N., Ikeuchi, M., and Inoue, Y. (1989) Biochim. Biophys. Acta, 973, 281–289.

    Google Scholar 

  6. Preston, C., and Seibert, M. (1991) Biochemistry, 30, 9615–9624.

    Google Scholar 

  7. Blubaugh, D. J., and Cheniae, G. M. (1992) Research in Photosynthesis, Vol. 2, Kluwer Academic Publishers, Dordrecht, The Netherlands, pp. 361–364.

    Google Scholar 

  8. Magnuson, A., and Andreasson, L.-E. (1997) Biochemistry, 36, 3254–3261.

    Google Scholar 

  9. Tamura, N., Noda, K., Wakamatsu, K., Kamachi, H., Inoue, H., and Wada, K. (1997) Plant Cell Physiol., 38, 578–585.

    Google Scholar 

  10. Ghirardi, M. L., Lutton, T. W., and Seibert, M. (1998) Biochemistry, 37, 13559–13566.

    Google Scholar 

  11. Ghirardi, M. L., Lutton, T. W., and Seibert, M. (1998) Biochemistry, 37, 13567–13574.

    Google Scholar 

  12. Chu, H. A., Nguyuen, A. P., and Debus, R. J. (1995) Biochemistry, 34, 5839–5858.

    Google Scholar 

  13. Chu, H. A., Nguyuen, A. P., and Debus, R. J. (1995) Biochemistry, 34, 5859–5882.

    Google Scholar 

  14. Boerner, R. J., Nguyen, A. P., Barry, B. A., and Debus, R. J. (1992) Biochemistry, 31, 6660–6672.

    Google Scholar 

  15. Nixon, P. J., and Diner, B. A. (1992) Biochemistry, 31, 19859–19871.

    Google Scholar 

  16. Vermaas, W. F. J., Charite, J., and Shen, G. (1990) Biochemistry, 29, 5325–5332.

    Google Scholar 

  17. Tang, X.-S., Diner, B. A., Larsen, B. S., Gilchrist, M. L., Lorigan, G. A., and Britt, R. D. (1994) Proc. Natl. Acad. Sci. USA, 91, 704–708.

    Google Scholar 

  18. Blubaugh, D. J., and Cheniae, G. M. (1990) Biochemistry, 29, 5109–5118.

    Google Scholar 

  19. Semin, B. K., Ivanov, I. I., Rubin, A. B., and Parak, F. (1995) FEBS Lett., 375, 223–226.

    Google Scholar 

  20. Ono, T., and Mino, H. (1999) Biochemistry, 38, 8778–8785.

    Google Scholar 

  21. Hsu, B.-D., Lee, J.-I., and Pan, R. L. (1987) Biochim. Biophys. Acta, 890, 89–96.

    Google Scholar 

  22. Ghirardi, M. L., Lutton, T. W., and Seibert, M. (1996) Biochemistry, 35, 1820–1828.

    Google Scholar 

  23. Govindjee (1996) Photosynthesis Res., 48, 117–126.

    Google Scholar 

  24. Ono, T., and Inoue, Y. (1991) FEBS Lett., 278, 183–186.

    Google Scholar 

  25. Semin, B. K., Davletshina, L. N., Ivanov, I. I., Reiner, M., and Parak, F. (1998) in Photosynthesis: Mechanisms and Effects (Garab, G., ed.) Vol. 2, Kluwer Academic Publishers, Dordrecht, The Netherlands, pp. 1415–1418.

    Google Scholar 

  26. Semin, B. K., and Parak, F. (1997) FEBS Lett., 400, 259–262.

    Google Scholar 

  27. Berthold, D. A., Babcock, G. T., and Yocum, C. F. (1981) FEBS Lett., 134, 231–234.

    Google Scholar 

  28. Solntsev, M. K., Ekobena, P. F., Karavaev, V. A., and Yurina, T. P. (1998) J. Luminescence, 76, 349–353.

    Google Scholar 

  29. Mamedov, F., Sayre, R. T., and Styring, S. (1998) Biochemistry, 37, 14245–14256.

    Google Scholar 

  30. Kramer, D. M., Roffey, R. A., Govindjee, and Sayre, R. T. (1994) Biochim. Biophys. Acta, 1185, 228–237.

    Google Scholar 

  31. Tamura, N., Noda, K., Wakamatsu, K., Kamachi, H., Inoue, H., and Wada, K. (1997) Plant Cell Physiol., 38, 578–585.

    Google Scholar 

  32. Ono, T., and Inoue, Y. (1991) Biochemistry, 30, 6183–6188.

    Google Scholar 

  33. Joliot, A. (1974) Biochim. Biophys. Acta, 357, 439–448.

    Google Scholar 

  34. Inoue, Y., and Shibata, K. (1978) FEBS Lett., 85, 193–197.

    Google Scholar 

  35. Hays, A. N., Vassiliev, I. R., Golbeck, J. H., and Debus, R. J. (1999) Biochemistry, 38, 11851–11865.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Kultisheva, M.Y., Lovyagina, E.R., Kuznetsov, A.M. et al. Comparative Study of Effects of Artificial Electron Donors on the AT-Band of Photosystem II Thermoluminescence. Biochemistry (Moscow) 66, 715–720 (2001). https://doi.org/10.1023/A:1010248309383

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1010248309383

Navigation