Hostname: page-component-586b7cd67f-t8hqh Total loading time: 0 Render date: 2024-11-24T01:33:16.908Z Has data issue: false hasContentIssue false
  • English
  • Français

Quantifying the Inhibitor-Target Site Interactions of Photosystem II Herbicides

Published online by Cambridge University Press:  12 June 2017

John L. Huppatz
John L. Huppatz*
Affiliation:
CSIRO Division of Plant Industry, GPO Box 1600, Canberra, ACT 2601, Australia
Get access Rights & Permissions [Opens in a new window]

Abstract

A convergence of research effort in a number of scientific disciplines in the early 1980s resulted in a rapid expansion of knowledge of the structure and function of the photosynthetic reaction center in bacteria and higher plants. The structure of the reaction center from photosynthetic bacteria was determined by X-ray analysis. The herbicide binding protein (the D1 protein) was identified by photoaffinity labelling and found to be an integral part of the photosynthetic reaction center complex in higher plants. Studies using herbicide-resistant mutants enabled the location of the herbicide binding niche on D1 to be determined. Quantitative Structure Activity Relationships (QSAR) of families of inhibitors and their effect on photosynthetic electron transport helped elucidate the nature of the interaction between inhibitors and receptor. Binding appeared to be predominantly hydrophobic with hydrogen bonding also having an important role. Studies with a series of highly potent inhibitors, the 2-cyanoacrylates, identified certain steric constraints in the interaction of these molecules with the binding site. The activity of these inhibitors was particularly sensitive to minor structural change and they proved to be useful probes of receptor topography. The results of structure-activity studies of the 2-cyanoacrylates combined with a refined knowledge of the three-dimensional structure of the inhibitor binding site has enabled computer-based molecular modelling of interactions of these inhibitors with the receptor. The spatial arrangement of the inhibitor functional groups within the binding domain was shown to be a critical factor in determining binding affinity.

Keywords

QSARcyanoacrylate inhibitorsmolecular modelling
Type
Symposium
Information
Weed Science , Volume 44 , Issue 3 , September 1996 , pp. 743 - 748
Copyright
Copyright © 1996 by the Weed Science Society of America 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Literature Cited

1. Bowyer, J., Hilton, M., Whitelegge, J., Jewess, P., Camilleri, P., Crofts, A., and Robinson, H. 1990. Molecular modelling studies on the binding of phenylurea inhibitors to the D1 protein of Photosystem II. Z. Naturforsch. 45c: 379–387.Google Scholar
2. Brown, B. T., Phillips, J. N., and Rattigan, B. M. 1981. 3-Alkoxyuracil derivatives. 2. Hill inhibitory activity. J. Agric. Food Chem. 29: 719–722.Google Scholar
3. Camilleri, P., Astles, D. P., Kerr, M. W., and Spencer, J. E. 1990. Aminopyrazolones: novel Photosystem II inhibitors. J. Agric. Food Chem. 38: 1601–1603.Google Scholar
4. Camilleri, P., Barker, M. D., Kerr, M. W., Whitehouse, M. K., Bowyer, J. R., and Lewis, R. J. 1989. Structure-activity studies on the inhibition of Photosystem II electron transport by phenylbiurets. J. Agric. Food Chem. 37: 1509–1513.Google Scholar
5. Camilleri, P., Bowyer, J. R., Gilkerson, T., Odell, B., and Weaver, R. C. 1987. Structure-activity relationships in the Hill inhibitory activity of substituted phenylureas. J. Agric. Food Chem. 35: 479–483.Google Scholar
6. Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. 1984. X-ray structure analysis of a membrane protein complex. J. Mol. Biol. 180: 385–398.Google Scholar
7. Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. 1985. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3Å resolution. Nature 318: 618–624.Google Scholar
8. Draber, W., Dickore, K., Buchel, K. H., Trebst, A., and Pistorius, E. 1968. Struktur-activität-korrelation bei 1,2,4-triazinonen, einer neuen gruppe von photosynthesehemmem. Naturwissenschaften 55: 446.Google Scholar
9. Fedtke, C. 1982. Biochemistry and Physiology of Herbicide Action. Springer Verlag, Berlin. Pages 18–60.Google Scholar
10. Gardner, G. 1981. Azidoatrazine: photoaffinity label for the site of triazine herbicide action in chloroplasts. Science 211: 937–940.Google Scholar
11. Gardner, G. and Sanborn, J. R. 1987. The role of chirality in the activity of Photosystem II herbicides. Z. Naturforsch. 42c: 663–669.Google Scholar
12. Hansch, C. and Deutsch, E. 1966. The structure-activity relationship in amides inhibiting photosynthesis. Biochim. Biophys. Acta. 112: 381–391.Google Scholar
13. Hansch, C. and Fujita, T. 1964. H-σ-π Analysis. A method for the correlation of biological activity and chemical structure. J. Amer. Chem. Soc. 86: 1616–1626.Google Scholar
14. Hirschberg, J., Bleeker, A., Kyle, D. J., McIntosh, L., and Arntzen, C. J. 1984. The molecular basis of triazine-herbicide resistance in higher-plant chloroplasts. Z. Naturforsch 39c: 412–420.Google Scholar
15. Hirschberg, J. and McIntosh, L. 1983. Molecular basis of herbicide resistance in Amaranthus hyhridus . Science 222: 1346–1348.CrossRefGoogle Scholar
16. Huppatz, J. L., McFadden, H. G., Huber, M-L., and McCaffery, L. F. 1992. Cyanoacrylate inhibitors of photosynthetic electron transport. Structural requirements for inhibitor potency and herbicidal activity. Pages 186–199 in Baker, D. R., Fenyes, J. G., and Steffens, J. J., eds. Synthesis and Chemistry of Agrochemicals III. ACS Symposium, Series 504. Amer. Chem. Soc., Washington, DC.Google Scholar
17. Huppatz, J. L. and McFadden, H. G. 1993. Understanding the topography of the Photosystem II herbicide binding niche: does QSAR help? Z. Naturforsch. 48c: 140–145.Google Scholar
18. Huppatz, J. L., McFadden, H. G., and McCaffery, L. F. 1990. Cyanoacrylate inhibitors as probes for the nature of the Photosystem II herbicide binding site. Z Naturforsch. 45: 336–342.Google Scholar
19. Huppatz, J. L., Phillips, J. N., and Rattigan, B. M. 1981. Cyanoacrylates. Herbicidal and photosynthetic inhibitory activity. Agric. Biol. Chem. 45: 2769–2773.Google Scholar
20. Huppatz, J. L. and Phillips, J. N. 1987. Stereospecific inhibitor probes of the PSII herbicide binding site. Z. Naturforsch. 42c: 674–678.Google Scholar
21. Huppatz, J. L. and Phillips, J. N. 1987. Cyanoacrylate inhibitors of the Hill reaction. IV. Binding characteristics of the hydrophobic domain. Z. Naturforsch. 42c: 679–683.Google Scholar
22. Huppatz, J. L. and Phillips, J. N. 1987. Cyanoacrylate inhibitors of the Hill reaction. V. The effect of chirality on inhibitor binding. Z Naturforsch 42c: 684–689.Google Scholar
23. Kakkis, E., Palmire, V. C. Jr., Strong, C. D., Bertsch, W., Hansch, C., and Schirmer, U. 1984. Quantitative structure-activity relationships in the inhibition of Photosystem II in chloroplasts by phenylureas. J. Agric. Food Chem. 32: 133–144.Google Scholar
24. Macdowall, F. D. 1949. The effects of some inhibitors of photosynthesis upon the photochemical reduction of a dye by isolated chloroplasts. Plant Physiol. 24: 462–480.Google Scholar
25. Mackay, S. P. and O'Malley, P. J. 1993. Molecular modelling of the interaction between DCMU and the QB-binding site of Photosystem II. Z. Naturforsch 48c: 191–198.Google Scholar
26. Mackay, S. P. and O'Malley, P. J. 1993. Molecular modelling of the interactions between optically active triazine herbicides and Photosystem II. Z. Naturforsch. 48c: 474–481.Google Scholar
27. Mackay, S. P. and O'Malley, P. J. 1993. Molecular modelling of the interaction of cyanoacrylate inhibitors with Photosystem II. Part 1. The effect of hydrophobicity of inhibitor binding. Z. Naturforsch. 48c:773–781.Google Scholar
28. Mackay, S. P. and O'Malley, P. J. 1993. Molecular modelling of the interaction of cyanoacrylate inhibitors with Photosystem II. Part 2. The effect of stereochemistry of inhibitor binding. Z. Naturforsch. 48c: 782–787.Google Scholar
29. McFadden, H. G., Craig, D. C., Huppatz, J. L., and Phillips, J. N. 1991. X–ray structure analysis of a cyanoacrylate inhibitor of Photosystem II electron transport. Z. Naturforsch. 46c: 93–98.Google Scholar
30. Michel, H. and Deisenhofer, J. 1988. Relevance of the photosynthetic reaction center from purple bacteria to the structure of Photosystem II. Biochem. 27: 1–7.Google Scholar
31. Mitsutake, K., Iwamura, H., Shimizu, R., and Fujita, T. 1986. Quantitative structure-activity relationship of Photosystem II inhibitors in chloroplasts and its link to herbicidal action. J. Agric. Food Chem. 34: 725–732.Google Scholar
32. Moreland, D. E. and Boots, M. R. 1971. Effects of optically active 1-(α-methylbenzyl)-3-(3,4-dichlorophenyl)urea on reactions of mitochondria and chloroplasts. Plant Physiol. 47: 53–58.Google Scholar
33. Pfister, K. and Arntzen, C. J. 1979. The mode of action of Photosystem II—specific inhibitors in herbicide-resistant weed biotypes. Z. Naturforsch. 34e: 996–1009.Google Scholar
34. Phillips, J. N. 1990. Hydrophilic Photosystem II inhibitors: cyanoacrylate thiolate salts. Z. Naturforsch. 45c: 343–347.Google Scholar
35. Soskic, M. and Sabljic, A. 1989. Inhibition of Hill reaction by 2-azido-s-triazine derivatives: QSAR study with molecular connectivity indices. Z. Naturforsch. 44c: 255–261.Google Scholar
36. Takemoto, I., Yoshida, R., Sumida, S., and Kamoshita, K. 1984. Quantitative structure-activity relationships of substituted phenylureas on the Hill inhibitory activity. J. Pest. Sci. 9: 517–521.Google Scholar
37. Tietjen, K. G., Draber, W., Goossens, J., Jansen, J. R., Kluth, J. F., Schindler, M., Wroblowsky, H. J., Hilp, U., and Trebst, A. 1993. Binding of triazines and triazinones in the QB-binding niche of Photosystem II. Z. Naturforsch. 48c: 205–212.Google Scholar
38. Tietjen, K. G., Kluth, J. F., Andree, R., Haug, M., Lindig, M., Müller, K. H., Wroblowsky, H. J., and Trebst, A. 1991. The herbicide binding niche of Photosystem II—a model. Pestic. Sci. 31: 65–72.Google Scholar
39. Tischer, W. and Strotmann, H. 1977. Relationship between inhibitor binding by chloroplasts and inhibition of photosynthetic electron transport. Biochim. Biophys. Acta. 460: 113–125.Google Scholar
40. Trebst, A. 1987. The three-dimensional structure of the herbicide binding niche on the reaction center polypeptides of Photosystem II. Z. Naturforsch. 42e: 742–750.CrossRefGoogle Scholar
41. Wessels, J.S.C. and van der Veen, R. 1956. The action of some derivatives of phenylurethan and of 3-phenyl-1, 1-dimethylurea on the Hill reaction. Biochim. Biophys. Acta. 19: 548–549.Google Scholar
42. Wolber, P. K. and Steinback, K. E. 1984. Identification of the herbicide binding region of the QB-protein by photoaffinity labelling with azidoatrazine. Z. Naturforsch. 39c: 425–429.Google Scholar
43. Zurawski, G., Bohnert, H. J., Whitfeld, P. R., and Bottomley, W. 1982. Nucleotide sequence of the gene for the Mr 32,000 thylakoid membrane protein from Spinacia oleracea and Nicotiana debneyi predicts a totally conserved primary translation product of Mr 38,950. Proc. Natl. Acad. Sci. U.S.A. 79: 7699–7703.Google Scholar