Works (3)
Updated: July 5th, 2023 15:54
2010 journal article
X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: Evidence for photoreductive dissociation of the iron-cyanide bond
Acta Crystallographica. Section D, Biological Crystallography, 66, 770–782.
Source: NC State University Libraries
Added: August 6, 2018
2009 journal article
Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 65, 34–40.
MeSH headings : Animals; Crystallization; Crystallography, X-Ray; Heme Oxygenase (Decyclizing) / chemistry; Heme Oxygenase (Decyclizing) / metabolism; Hemoglobins / chemistry; Hemoglobins / metabolism; Histidine / chemistry; Histidine / metabolism; Iodobenzenes / chemistry; Iodobenzenes / metabolism; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Protein Binding; Protein Conformation; Solvents
TL;DR:
It is reported that the distal histidine, His55, exhibits conformational flexibility in the deoxy form and is consequently observed in two solvent-exposed conformations more than 9.5 A away from the heme, analogous to the open conformation of sperm whale myoglobin.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2007 journal article
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 63, 1094–1101.
MeSH headings : Animals; Binding Sites; Crystallography, X-Ray / methods; Cysteine / chemistry; Escherichia coli / metabolism; Heme / chemistry; Hemoglobins / chemistry; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Conformation; Peroxidases / chemistry; Polychaeta / metabolism; Protein Conformation; Recombinant Proteins / chemistry; Serine / chemistry
TL;DR:
Hydrogen-bonding interaction between His55 and the bound diatomic oxygen molecule provides new insight into the catalytic activation of H(2)O(2), which is essential for peroxidase activity.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
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