51V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site-Reference-Cited by-同舟云学术

51V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site

Published:2015-04-20 Issue:16 Volume:137 Page:5618-5628
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Gupta Rupal¹,Hou Guangjin¹,Renirie Rokus²,Wever Ron²,Polenova Tatyana¹

Affiliation:

1. Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States

2. Van’t Hoff Institute for Molecular Science, University of Amsterdam, POSTBUS 94157, 1090 GD, Amsterdam, The Netherlands

Funder

United States - Israel Binational Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.5b02635

Reference72 articles.

1. Vanadium chloroperoxidases occur widely in nature

2. Mechanistic considerations of the vanadium haloperoxidases

3. cWever, R.InVanadium: Biochemical and Molecular Biological Approaches;Michibata, H., Ed.Springer Science+Business Media B.:New York, 2012; pp95–125.

4. The Stability and Steady-State Kinetics of Vanadium Chloroperoxidase from the Fungus Curvularia Inaequalis

5. X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis

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