Chelsea E. Chaudhary

Works (1)

Updated: July 11th, 2023 20:10

2006 journal article

Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase

BIOCHEMISTRY, 45(30), 9085–9094.

By: S. Franzen n , J. Belyea n, L. Gilvey n, M. Davis n, C. Chaudhary n, T. Sit n , S. Lommel n

Contributors: S. Franzen n , J. Belyea n, L. Gilvey n, M. Davis n, C. Chaudhary n, T. Sit n , S. Lommel n

MeSH headings : Animals; Binding Sites / genetics; Hemoglobins; Histidine / chemistry; Histidine / genetics; Hydrogen Bonding; Mutagenesis, Site-Directed; Peroxidases / chemistry; Peroxidases / genetics; Peroxidases / metabolism; Phenylalanine / genetics; Polychaeta / enzymology; Polychaeta / genetics; Substrate Specificity / genetics; Tyrosine / genetics; Valine / genetics
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: The role of tyrosine 38 (Y38), which hydrogen bonds to the hydroxyl group of the substrate, was probed and it was suggested that abolishing this hydrogen bond may open a pathway for the escape of the one-electron product, the phenoxy radical leading to polymeric products. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries, ORCID
Added: August 6, 2018

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