Biochemistry

The mechanism of oxidative halophenol dehalogenation by Amphitrite ornata dehaloperoxidase is initiated by H2O2 binding and involves two consecutive one- …

RL Osborne, MK Coggins, GM Raner, M Walla…

Index: Osborne, Robert L.; Raner, Gregory M.; Hager, Lowell P.; Dawson, John H. Journal of the American Chemical Society, 2006 , vol. 128, # 4 p. 1036 - 1037

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Citation Number: 44

Abstract

The enzymatic globin, dehaloperoxidase (DHP), from the terebellid polychaete Amphitrite ornata is designed to catalyze the oxidative dehalogenation of halophenol substrates. In this study, the ability of DHP to catalyze this reaction by a mechanism involving two consecutive one-electron steps via the normal order of addition of the oxidant cosubstrate (H2O2) before organic substrate [2, 4, 6-trichlorophenol (TCP)] is demonstrated. Specifically, 1 equiv of ...