Autocatalytic Modification of the Prosthetic Heme of Horseradish but Not Lactoperoxidase by Thiocyanate Oxidation Products. A Role for Heme−Protein Covalent Cross-Linking-Reference-Cited by-同舟云学术

Autocatalytic Modification of the Prosthetic Heme of Horseradish but Not Lactoperoxidase by Thiocyanate Oxidation Products. A Role for Heme−Protein Covalent Cross-Linking

Published:2005-10-19 Issue:45 Volume:127 Page:15871-15879
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Wojciechowski Grzegorz¹,Huang Liusheng¹,Ortiz de Montellano Paul R.¹

Affiliation:

1. Contribution from the Department of Pharmaceutical Chemistry, University of California, 600 16th Street, San Francisco, California 94143-2280

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja054084t

Reference49 articles.

1. Eosinophil Peroxidase Oxidation of Thiocyanate

2. Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity.

3. Bactericidal and cytotoxic effects of hypothiocyanite-hydrogen peroxide mixtures

4. Inhibition of herpes simplex virus type 1, respiratory syncytial virus and echovirus type 11 by peroxidase-generated hypothiocyanite

5. X-ray crystal structure of canine myeloperoxidase at 3 Å resolution

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