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

Full Text: HTML

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 ...

Related Articles:

Photochemical rearrangement of chlorinated dibenzo-p-dioxins. Regioselective carbon-oxygen bond homolysis from the singlet excited state, and carbon-chlorine …

[Kobayashi, Takanori; Shimada, Jun-Ichi; Kitahara, Chieko; Haga, Naoki Chemistry Letters, 2006 , vol. 35, # 4 p. 348 - 349]

Electron-transfer oxidation of chlorophenols by uranyl ion excited state in aqueous solution. Steady-state and nanosecond flash photolysis studies

[Sarakha, Mohamed; Bolte, Michele; Burrows, Hugh D. Journal of Physical Chemistry A, 2000 , vol. 104, # 14 p. 3142 - 3149]

Ferroelectric oxides with strong visible-light absorption from charge ordering

[Clark, Joanna H.; Dyer, Matthew S.; Palgrave, Robert G.; Ireland, Christopher P.; Darwent, James R.; Claridge, John B.; Rosseinsky, Matthew J. Journal of the American Chemical Society, 2011 , vol. 133, # 4 p. 1016 - 1032]

More Articles...