The Mechanism of Oxidative Halophenol Dehalogenation by Amphitrite ornata Dehaloperoxidase Is Initiated by H2O2 Binding and Involves Two Consecutive One-Electron Steps: Role of Ferryl Intermediates-Reference-Cited by-同舟云学术

The Mechanism of Oxidative Halophenol Dehalogenation by Amphitrite ornata Dehaloperoxidase Is Initiated by H2O2 Binding and Involves Two Consecutive One-Electron Steps: Role of Ferryl Intermediates

Published:2009-04-29 Issue:20 Volume:48 Page:4231-4238
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Osborne Robert L.¹,Coggins Michael K.¹,Raner Gregory M.²,Walla Mike¹,Dawson John H.¹³

Affiliation:

1. Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208

2. Department of Chemistry and Biochemistry, University of North Carolina, Greensboro, North Carolina 27402

3. School of Medicine, University of South Carolina, Columbia, South Carolina 29208

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi900367e

Reference41 articles.

1. Osborne, R. L. (2006) Spectroscopic, kinetic, and mechanistic studies of the peroxide-dependent oxidative dehalogenation of halophenols catalyzed by heme proteins: From peroxidases to globins. Ph.D. Thesis,University of South Carolina,Columbia, SC

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

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

4. An enzymatic globin from a marine worm

5. Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase.

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