2009 journal article

Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata

BIOCHEMISTRY, 48(10), 2164–2172.

By: M. Davis n, H. Gracz n, F. Vendeix n, V. Serrano n, A. Somasundaram n, S. Decatur n, S. Franzen n

MeSH headings : Animals; Binding Sites / physiology; Catalysis; Catalytic Domain / physiology; Heme / chemistry; Hemoglobins / chemistry; Hemoglobins / genetics; Hemoglobins / metabolism; Hydrocarbons, Halogenated / chemistry; Hydrocarbons, Halogenated / metabolism; Molecular Conformation; Nuclear Magnetic Resonance, Biomolecular; Peroxidases / chemistry; Peroxidases / genetics; Peroxidases / metabolism; Phenols / chemistry; Phenols / metabolism; Polychaeta / enzymology; Polychaeta / genetics; Potassium Cyanide / chemistry; Protein Binding / physiology; Protein Conformation; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Substrate Specificity
TL;DR: The most soluble trihalogenated phenol acts as a highly soluble structural analogue to the native substrate 2,4,6-tribromophenol, and to improve the understanding of substrate binding, the most soluble substrate analogues are compared. (via Semantic Scholar)
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Added: August 6, 2018

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