2012 journal article

Study of the electrostatic effects of mutations on the surface of dehaloperoxidase-hemoglobin A

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 420(4), 733–737.

By: J. Zhao n, J. Rowe n, J. Franzen n, C. He* & S. Franzen n

author keywords: Surface mutation; Electrostatic interaction; Isoelectric focusing; Ionic strength effect; Enzyme kinetics
MeSH headings : Animals; Hemoglobin A / chemistry; Hemoglobin A / genetics; Mutagenesis; Mutation; Peroxidases / chemistry; Peroxidases / genetics; Polychaeta / enzymology; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Static Electricity
TL;DR: The electrostatic nature of substrate binding was further confirmed by the result that kinetic assays of DHP A were affected by ionic strength, and isoelectric focusing gel study showed that D HP A has a slight negative charge pH 7, consistent with the kinetic observations. (via Semantic Scholar)
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Added: August 6, 2018

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