Oxidative dechlorination of halogenated phenols catalyzed by two distinct enzymes: Horseradish peroxidase and dehaloperoxidase.
Arch Biochem Biophys
; 505(1): 22-32, 2011 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-20869943
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peroxidases
/
Fenóis
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Poliquetos
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Armoracia
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Halogenação
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Peroxidase do Rábano Silvestre
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article