Atrazine Inhibition of Photosystem II is Modulated By Specific Inorganic Cofactors Involved in Oxygen Evolution

  • Abdur Rashid
  • Robert Carpentier


The photosynthetic oxygen evolving complex is located toward the inner surface of the thylakoid and includes three extrinsic polypeptides of approximate molecular weights 16, 23 and 33 kDa. Three inorganic cofactors namely Cl, Ca2+ and Mn2+ are also established to be associated with the oxygen evolving complex (for a review see ref. 1). However, the relationships between the extrinsic polypeptides and the above inorganic components are not clearly understood. it is assumed that 33 kDa polypeptide is probably essential for maintaining the function of Mn atoms (2) and 23 and 16 kDa polypeptides are essential for functional stabilization of Cl and Ca2+ (3). Ca2+ and Mn2+ are however, supposed to be ligated to the residual portion of the D1 and/or D2 polypeptide at the water splitting side of photosystem II (PSII) (4). The D1 polypeptide also named as 32 kDa protein of QB-protein is well known for its binding site of many herbicides on the acceptor side of PSII at the level of QB (5).


Native Conformation Donor Side PSII Complex Atrazine Concentration Approximate Molecular Weight 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Homann, P.H. (1987) J. Bioenerg. Biomemb. 19, 105–123CrossRefGoogle Scholar
  2. 2.
    Ono, T.-A. and Inoue, Y. (1983) FEBS Lett. 164, 255–260.CrossRefGoogle Scholar
  3. 3.
    Murata, N. and Miyao, M. (1987) in Progress in Photosynthesis Research (Beggins, J. ed.) I, pp. 453–462, Martinus Nijhoff Publishers, DordrechtGoogle Scholar
  4. 4.
    Dismukes, G.C. (1988) Chemica Scripta 28A, 99–104Google Scholar
  5. 5.
    Van Rensen, J.J.S. (1982) Physiol. Plant 54, 515–521CrossRefGoogle Scholar
  6. 6.
    Berthold, D.A., Babcolk, G.T. and Yocum, C.F. (1981) FEBS Lett. 134, 231–234CrossRefGoogle Scholar
  7. 7.
    Nakatani, H.Y. (1984) Biochem. Biophys. Res. Comm. 120, 299–304PubMedCrossRefGoogle Scholar
  8. 8.
    Kuwabara, T. and Murata, N. (1983) Plant Cell Physiol. 24, 741–747Google Scholar
  9. 9.
    Seibert, M., Cotton, T.M. and Metz, J.G. (1988) Biochim. Biophys. Acta 934, 235–246CrossRefGoogle Scholar
  10. 10.
    Carpentier, R., Fuerst, E.P., Nakatani, H, and Arntzen, C.J. (1985) Biochim. Biophys. Acta 808, 293–299CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Abdur Rashid
    • 1
  • Robert Carpentier
    • 1
  1. 1.Centre de recherche en photobiophysiqueUniversité du Québec à Trois-RivièresTrois-RivièresCanada

Personalised recommendations