Measurement of Internal Substrate Binding in Dehaloperoxidase–Hemoglobin by Competition with the Heme–Fluoride Binding Equilibrium
Zhao, J., Moretto, J., Le, P., & Franzen, S. (2015, January 22). The Journal of Physical Chemistry B, Vol. 119, pp. 2827–2838.
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
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Neonatal Health and Biochemistry
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.
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