• Korean Journal of Weed Science
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• v.13 no.2
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• pp.81-88
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• 1993

For searching the photosynthetic electron transport(PET) inhibitors, bio-rational screening system using thylakoid membranes extracted from wild and mutant cyanobacteria(Anacystis nidulans $R_2$) was developed. Generally, thylakoid membrane was more sensitive to the tested herbicides than the chloroplast from spinach in the Hill reaction. Higher resistant characteristics appeared in mutant D-5, Di-22 to diuron and mutant G-264 to atrazine as compared to wild type. To test the reaction of thylakoid membrane to herbicides, diuron and atrazine were applied simultaneously. Diuron and atrazine competed each other for binding with substituted amino acids, while diuron and dinoseb were non-competitive, and inhibiting activity was increased. Conclusively, bio-rational screening system using cyanobacteria was proved to be fast and efficient screening method for the development of PET inhibitors.

• Korean Journal of Weed Science
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• v.13 no.2
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• pp.89-95
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• 1993

The Inhibiting activity of newly synthesized phenol (E-series) and triazine (T-series) derivatives was evaluated by using thylakoid membranes extracted from cyanobacteria (Anacystis nidulans $R_2$). There were no significant differences between phenol derivatives and dinoseb to the thylakoid membrane extracted from wild type in the Hill reaction. However, a phenol derivative, E-24 which has no -Cl at phenyl ring, did not show any activity. The longer the length of R substituents was in phenol derivatives, the lower inhibiting activity was in the Hill reaction. Triazine derivatives, T-27, T-28, T-40, T-41, T-47 and T-48 were also compared with diuron and atrazine. Among triazine compounds, T-27 and T-28 showed 10 and 30 times activity as high as atrazine to wild type, respectively. Other triazine derivatives, T-40, T-41, T-47 and T-48 showed low inhibiting activity to wild and mutant type. A structural difference of T-27 and T-28 from T-40, T-41, T-47 and T-48 was the presented of -C-NH-. Both T-27 and T-28 were very closely associated with serine, an amino acid located at the 264th position of D1 protein because of the resistant ratio(R/S) to mutant G-264 were higher than that of atrazine.