Reversible Inhibition of DCMU on the Oxidizing Side of Photosystem II

  • Hiroshi Inoué
  • Hiroyuki Kamachi
  • Tohoru Kitamura
  • Noriaki Tamura

Abstract

Two sites of inhibition in photosystem II (PS II) have been shown for 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU). The primary inhibition site which has been well characterized is localized at Q, which is harbored by D1 protein (1). The second inhibition site of DCMU has been reported to exist on the oxidizing side of PS II in chloroplasts (2, 3) or Triton-prepared PS II membranes (4,5). However, it remains to be solved which species on the oxidizing side of PSII react(s) with EXMJ in detail, since it is very difficult to distinguish between two inhibitions by the herbicide. Interestingly, results have been accumulated that D1 protein possesses functional components of the oxidizing side of PS II such as the Mn ligation site (6), Z and D (7), and P680 (8), in addition to those on the PS II reducing side. In this report, with Tris-treated PS II membranes (Tris-TMF2), we confirmed the dual inhibitions by DCMU of PS II, and found that DCMU modifies the high-affinity Mn-binding site, resulting in the inhibition of photoligation of Mn2+ into the apo-Mn complex.

Keywords

Chlorophyll Fluorescence Oxygen Evolution Inhibition Site PSII Membrane Diphenyl Carbazide 
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.

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References

  1. 1.
    Trebst, A. (1987) Z. Naturforsch. 42c, 742–750Google Scholar
  2. 2.
    Renger, G. (1973) Biochim. Biophys. Acta 314, 113–116PubMedCrossRefGoogle Scholar
  3. 3.
    Bouges-Bocquet, B., Bennoun, P. and Taboury, J. (1973) Biochim, Biophys. Acta 325, 247–254CrossRefGoogle Scholar
  4. 4.
    Carpentier, R., Fuerst, E.P., Nakatani, H.Y. and Arntzen, C.J. (1985) Biochim. Biophys. Acta 808, 293–299CrossRefGoogle Scholar
  5. 5.
    Hsu, B.D., Lee, J.Y. and Pan, R.L. (1986) Biochem. Biophys. Res. Commun. 141, 682–688PubMedCrossRefGoogle Scholar
  6. 6.
    Tamura, N., Ikeuchi, M. and Inoue, Y. (1989) Biochim. Biophys. Acta 973, 281–289CrossRefGoogle Scholar
  7. 7.
    Debus, R.J., Barry, B.A., Babcock, G.T. and Mcintosh, L. (1988) Proc. Natl. Acad. Sci. USA 85, 427–430PubMedCrossRefGoogle Scholar
  8. 8.
    Nanba, O. and Satoh, K. (1987) Proc. Natl. Acad. Sci. USA 84, 109–112PubMedCrossRefGoogle Scholar
  9. 9.
    Tamura, N. and Cheniae, G. (1987) Biochim. Biophys. Acta 890, 179-194CrossRefGoogle Scholar
  10. 10.
    Inoué, H. and Wada, T. (1987) Plant Cell Physiol. 28, 767–773Google Scholar
  11. 11.
    Inoué, H., Kaneko, M. and Kitamura, T. (1987) Photosynthetica 21, 591–594Google Scholar
  12. 12.
    Metz, J.G., Pakrasi, H.B., Seibert, M. and Arntzen, C.J. (1986) FEBS Lett. 205, 269–274CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Hiroshi Inoué
    • 1
  • Hiroyuki Kamachi
    • 1
  • Tohoru Kitamura
    • 1
  • Noriaki Tamura
    • 1
  1. 1.Department of Biology, Faculty of ScienceToyama UniversityToyama 930Japan

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