General H. Hugh Shelton Leadership Center

Works Published in 2010

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2010 journal article

Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function

BIOPHYSICAL JOURNAL, 99(5), 1586–1595.

By: M. Thompson n, M. Davis n, V. Serrano n, F. Nicoletti*, B. Howes*, G. Smulevich*, S. Franzen n

MeSH headings : Animals; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors / chemistry; Enzyme Inhibitors / metabolism; Enzyme Inhibitors / pharmacology; Halogenation; Hemoglobins / chemistry; Hemoglobins / metabolism; Iodobenzenes / chemistry; Iodobenzenes / metabolism; Iodobenzenes / pharmacology; Kinetics; Models, Molecular; Peroxidases / antagonists & inhibitors; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Spectrum Analysis, Raman
TL;DR: It is demonstrated that DHP has a unique two-site competitive binding mechanism in which the internal and external binding sites communicate through two conformations of the distal histidine of the enzyme, resulting in nonclassical competitive inhibition. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2010 journal article

X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: Evidence for photoreductive dissociation of the iron-cyanide bond

Acta Crystallographica. Section D, Biological Crystallography, 66, 770–782.

Source: NC State University Libraries
Added: August 6, 2018

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