General H. Hugh Shelton Leadership Center

Works Published in 2006

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2006 journal article

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

BIOCHEMISTRY, 45(30), 9085–9094.

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
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)
UN Sustainable Development Goal Categories
14. Life Below Water (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

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