The Mammalian Cytosolic Selenoenzyme Thioredoxin Reductase Reduces Ubiquinone-Reference-Cited by-同舟云学术

The Mammalian Cytosolic Selenoenzyme Thioredoxin Reductase Reduces Ubiquinone

Published:2003-01 Issue:4 Volume:278 Page:2141-2146
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Xia Ling,Nordman Tomas,Olsson Jerker M.,Damdimopoulos Anastassios,Björkhem-Bergman Linda,Nalvarte Ivan,Eriksson Lennart C.,Arnér Elias S.J.,Spyrou Giannis,Björnstedt Mikael

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference35 articles.

1. Chemistry and Biochemistry of Flavoenzyme;Williams,1992

2. Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

3. Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme

4. Essential Role of Selenium in the Catalytic Activities of Mammalian Thioredoxin Reductase Revealed by Characterization of Recombinant Enzymes with Selenocysteine Mutations

5. Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity

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