The Selenium-independent Inherent Pro-oxidant NADPH Oxidase Activity of Mammalian Thioredoxin Reductase and Its Selenium-dependent Direct Peroxidase Activities-Reference-Cited by-同舟云学术

The Selenium-independent Inherent Pro-oxidant NADPH Oxidase Activity of Mammalian Thioredoxin Reductase and Its Selenium-dependent Direct Peroxidase Activities

Published:2010-07 Issue:28 Volume:285 Page:21708-21723
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cheng Qing,Antholine William E.,Myers Judith M.,Kalyanaraman Balaraman,Arnér Elias S.J.,Myers Charles R.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference72 articles.

1. Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions

2. Physiological functions of thioredoxin and thioredoxin reductase

3. Properties and Biological Activities of Thioredoxins

4. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system1 1This review is based on the licentiate thesis “Thioredoxin reductase—interactions with the redox active compounds 1-chloro-2,4-dinitrobenzene and lipoic acid” by Jonas Nordberg, 2001, Karolinska Institute, Stockholm, ISBN 91-631-1064-4.

5. Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen

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