Zuxu Chen

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.

By: V. Serrano, M. Davis, J. Gaff, Q. Zhang, Z. Chen, E. D'Antonio, E. Bowden , R. Rose , S. Franzen 

Source: NC State University Libraries
Added: August 6, 2018

2008 article

Distal histidine conformational flexibility in dehaloperoxidase fromAmphitrite ornata

Chen, Z., Serrano, V., Betts, L., & Franzen, S. (2008, December 17). Acta Crystallographica Section D Biological Crystallography, Vol. 65, pp. 34–40.

By: Z. Chen n, V. Serrano n, L. Betts * & S. Franzen n 

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
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
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)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2007 article

X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned fromAmphitrite ornata

Serrano, V., Chen, Z., Davis, M. F., & Franzen, S. (2007, September 19). Acta Crystallographica Section D Biological Crystallography, Vol. 63, pp. 1094–1101.

By: V. Serrano n, Z. Chen n, M. Davis n & S. Franzen n 

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
topics (OpenAlex): Hemoglobin structure and function; Porphyrin Metabolism and Disorders; Heme Oxygenase-1 and Carbon Monoxide
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)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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