A Novel Multistep Mechanism for Oxygen Binding to Ferrous Hemoproteins: Rapid Kinetic Analysis of Ferrous-Dioxy Myeloperoxidase (Compound III) Formation-Reference-Cited by-同舟云学术

A Novel Multistep Mechanism for Oxygen Binding to Ferrous Hemoproteins: Rapid Kinetic Analysis of Ferrous-Dioxy Myeloperoxidase (Compound III) Formation

Published:2004-08-20 Issue:36 Volume:43 Page:11589-11595
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Abu-Soud Husam M.¹,Raushel Frank M.¹,Hazen Stanley L.¹

Affiliation:

1. Department of Obstetrics and Gynecology, The C.S. Mott Center for Human Growth and Development, 275 E. Hancock, Detroit, Michigan 48201, Department of Biochemistry and Molecular Biology, Wayne State University, Detroit, Michigan 48201, Department of Chemistry, Texas A&M University, College Station, Texas 77842, and Departments of Cell Biology and Cardiovascular Medicine and Center for Cardiovascular Diagnostics and Prevention, Cleveland Clinic Foundation, Cleveland, Ohio 44195

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi049541h

Reference62 articles.

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2. 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima.

3. Oxidants and antioxidants in the pathogenesis of atherosclerosis: implications for the oxidized low density lipoprotein hypothesis

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