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Inhibition of Plant Acetolactate Synthase by Nicosulfuron, Rimsulfuron, and Their Mixture DPX-79406

Published online by Cambridge University Press:  12 June 2017

Mounir Mekki
Affiliation:
Dep. Phytologie, Univ. Laval, Ste-Foy, Qc, G1K 7P4, Canada
Gilles D. Leroux
Affiliation:
Dep. Phytologie, Univ. Laval, Ste-Foy, Qc, G1K 7P4, Canada

Abstract

Nicosulfuron and rimsulfuron are two selective postemergence sulfonylurea herbicides commercialized, respectively, in Europe and USA for weed control in maize. They are under development in Canada as a 1:1 premix (DPX-79406). The objective of the present study was to investigate the effects of these herbicides and their interactions on acetolactate synthase (ALS) activity of selected annual weed species. Each nicosulfuron and rimsulfuron treatment used over a concentration range of 0.01 to 10 μM produced a distinct pattern of ALS inhibition for common ragweed, proso millet, redroot pigweed, smooth crabgrass, and wild oats. Based on ALS specific activity, I50 values for each herbicide differed slightly among the five weed species. However, rimsulfuron was much more inhibitory to ALS than was nicosulfuron. Common ragweed ALS activity increased linearly from 30 to 120 min, even in the continual presence of both herbicides in the assay buffer. This suggests the reversibility of their interaction with ALS. Delaying nicosulfuron (1 μM) or rimsulfuron (0.1 μM) additions to the assay buffer, after initiating the reaction with the enzyme, resulted in a quadratic increase of common ragweed ALS activity. In the continual presence of 0.1 μM of rimsulfuron, addition of 0.1 or 1 μM nicosulfuron did not affect ALS activity any further. However, in the continual presence of 0.1 μM of nicosulfuron, delaying rimsulfuron addition caused an increase in ALS activity. This increase was lower in the presence of 1 μM of nicosulfuron. Inhibition of common ragweed ALS by nicosulfuron and rimsulfuron was not independent of each other, suggesting some competition between the two herbicides for a common binding site on ALS.

Type
Physiology, Chemistry, and Biochemistry
Copyright
Copyright © 1994 by the Weed Science Society of America 

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