Probing the Oxyferrous and Catalytically Active Ferryl States of Amphitrite ornata Dehaloperoxidase by Cryoreduction and EPR/ENDOR Spectroscopy. Detection of Compound I-Reference-Cited by-同舟云学术

Probing the Oxyferrous and Catalytically Active Ferryl States of Amphitrite ornata Dehaloperoxidase by Cryoreduction and EPR/ENDOR Spectroscopy. Detection of Compound I

Published:2010-10-06 Issue:42 Volume:132 Page:14995-15004
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Davydov Roman¹,Osborne Robert L.¹,Shanmugam Muralidharan¹,Du Jing¹,Dawson John H.¹,Hoffman Brian M.¹

Affiliation:

1. Department of Chemistry, Northwestern University, Evanston, Illinois 60208, and Department of Chemistry and Biochemistry and School of Medicine, University of South Carolina, Columbia, South Carolina 29208

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja1059747

Reference56 articles.

1. An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata

2. The Crystal Structure and Amino Acid Sequence of Dehaloperoxidase from Amphitrite ornata Indicate Common Ancestry with Globins

3. An enzymatic globin from a marine worm

4. Notomastus lobatus Chloroperoxidase and Amphitrite ornata Dehaloperoxidase Both Contain Histidine as Their Proximal Heme Iron Ligand

5. The Unusual Reactivities of Amphitrite ornata Dehaloperoxidase and Notomastus lobatus Chloroperoxidase Do Not Arise from a Histidine Imidazolate Proximal Heme Iron Ligand

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