Oxidative dechlorination of halogenated phenols catalyzed by two distinct enzymes: Horseradish peroxidase and dehaloperoxidase |
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Authors: | Lukasz Szatkowski Matthew K Thompson Rafal Kaminski Stefan Franzen Agnieszka Dybala-Defratyka |
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Institution: | aTechnical University of Lodz, Faculty of Chemistry, Institute of Applied Radiation Chemistry, Zeromskiego 116, 90-924 Lodz, Poland;bNorth Carolina State University, Department of Chemistry, Raleigh, NC 27695, USA |
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Abstract: | The mechanism of the dehalogenation step catalyzed by dehaloperoxidase (DHP) from Amphitrite ornata, an unusual heme-containing protein with a globin fold and peroxidase activity, has remarkable similarity with that of the classical heme peroxidase, horseradish peroxidase (HRP). Based on quantum mechanical/molecular mechanical (QM/MM) modeling and experimentally determined chlorine kinetic isotope effects, we have concluded that two sequential one electron oxidations of the halogenated phenol substrate leads to a cationic intermediate that strongly resembles a Meisenheimer intermediate – a commonly formed reactive complex during nucleophilic aromatic substitution reactions especially in the case of arenes carrying electron withdrawing groups. |
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Keywords: | Dehaloperoxidase Horseradish peroxidase Chlorine kinetic isotope effects QM/MM Halophenols Oxidation |
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