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

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Human Thioredoxin Reductase Directly Reduces Lipid Hydroperoxides by NADPH and Selenocystine Strongly Stimulates the Reaction via Catalytically Generated Selenols

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Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase

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1-Chloro-2,4-dinitrobenzene Is an Irreversible Inhibitor of Human Thioredoxin Reductase

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Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin

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