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Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata

โœ Scribed by Zhao, Jing; de Serrano, Vesna; Zhao, Junjie; Le, Peter; Franzen, Stefan


Book ID
120456040
Publisher
American Chemical Society
Year
2013
Tongue
English
Weight
477 KB
Volume
52
Category
Article
ISSN
0006-2960

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โœ de Serrano, Vesna ;Chen, Zuxu ;Davis, Michael F. ;Franzen, Stefan ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› International Union of Crystallography ๐ŸŒ English โš– 953 KB

The dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata is an enzyme that converts para-halogenated phenols to the corresponding quinones in the presence of hydrogen peroxide. Its enzymatic activity is similar to that of heme peroxidases such as horseradish peroxidase, yet it has