Enzyme-Kinetic Studies on the Interaction of Norflurazon with Phytoene Desaturase

Abstract

Bleaching herbicides inhibit carotene biosynthesis in photosynthetic organisms. The interaction of norflurazon [4-chloro-5-methylamino-2-(3-trifluoromethylphenyl)-pyridazin-3(2H)one] with its target enzyme phytoene desaturase, has been characterized by enzyme-kinetic studies. A Lineweaver-Burk plot showed a non-competitive m anner for norflurazon inhibition. Binding of norflurazon to phytoene desaturase was reversible as dem onstrated by complete replacem ent of bound 14C-labeled herbicide by unlabeled norflurazon. In a linear Dixon plot the ki value for norflurazon was determ ined as 0.09 μм . With the in vitro system from Anacystis used in this study it was possible to perform structure-activity studies with selected m -phenyl-substituted pyridazinones. A linear relationship between inhibitory properties of these compounds and their lipophilicity could be established.