2015 journal article

Measurement of Internal Substrate Binding in Dehaloperoxidase-Hemoglobin by Competition with the Heme-Fluoride Binding Equilibrium


By: J. Zhao n, J. Moretto n, P. Le n & S. Franzen n

MeSH headings : Amino Acids / chemistry; Animals; Anions / chemistry; Binding Sites; Binding, Competitive; Fluorides / chemistry; Halogenation; Heme / chemistry; Hemoglobins / chemistry; Hydrogen Bonding; Hydrogen-Ion Concentration; Indoles / chemistry; Peroxidases / chemistry; Phenols / chemistry; Polychaeta; Protein Binding; Spectrum Analysis
TL;DR: 2, 4-dibromophenol (2,4-DBP) is identified as the tightest binding substrate discovered thus far, with approximately 20-fold tighter binding affinity than that of 4-bromophenols (4-BP), a known internally binding inhibitor in DHP. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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