No Selenium Required: Reactions Catalyzed by Mammalian Thioredoxin Reductase That Are Independent of a Selenocysteine Residue
Author:
Affiliation:
1. Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi802146w
Reference53 articles.
1. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli
2. Thioredoxin reductase
3. Rat and Calf Thioredoxin Reductase Are Homologous to Glutathione Reductase with a Carboxyl-terminal Elongation Containing a Conserved Catalytically Active Penultimate Selenocysteine Residue
4. Selenocysteine: the 21st amino acid
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