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United States Department of Agriculture

Agricultural Research Service

Title: Amino and Urea-Substituted Thiazoles Inhibit Photosynthetic Electron Transfer

Authors
item Dayan, Franck
item Vincent, Armelle - UNIV OF BURGUNDY,FRANCE
item Romagni, Joanne
item Allen, Stacy
item Duke, Stephen
item Duke, Mary
item Bowling, John - UNIV OF MISSISSIPPI
item Zjawiony, Jordan - UNIV OF MISSISSIPPI

Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: March 15, 2000
Publication Date: N/A

Interpretive Summary: 3 series of thiazole analogues were synthesized. Our study shows that some of the compounds acted like herbicides and inhibited photosynthesis. We demonstrated that the active molecules stopped the flow of electron by competing for the binding site of the natural electron acceptor on the protein. We also used computer modeling to determine what portion of the molecules were required for biological activity.

Technical Abstract: Protoporphyrinogen oxidase (Protox) is the target site of a large number of commercial herbicides. Previous QSARs performed at a 2-dimensional (2-D) level reproduced the activity of individual data sets relatively well, but these models could not be used to predict the activity of structurally related derivatives. We developed a more reliable model by applying 3-dimensional (3-D) molecular techniques to a set of 31 phenyl ether (PE) analogues. Inhibitory activity at the molecular site of action was chosen because it circumvents the effects of uptake, translocation, and metabolism of the compounds occurring in whole plant studies. Increased predictability was achieved by aligning the diphenyl ether (DPE) analogues along the trifluoromethyl phenyl (q2=0.70) ring rather than along the nitrophenyl (q2=0.65) ring or along the centroids (q2=0.69). This new analysis differentiated between R and S enantiomers and allowed the prediction of the inhibitory activity of the natural diphenyl ether cyperine. The prediction model suggests that the binding of cyperine on the active site of Protox is stereospecific.

Last Modified: 11/26/2014
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