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

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 6, 2000, Pages 2521-2526

  Lee, Seung Rock ^a   Bar Noy, Shoshana ^a   Kwon, Jaeyul ^a   Levine, Rodney L ^a   Stadtman, Thressa C ^a   Rhee, Sue Goo ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SELENIUM; SELENOCYSTEINE; SULFUR; THIOREDOXIN REDUCTASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; MAMMAL; NONHUMAN; OXIDATION; PRIORITY JOURNAL;

ANIMALS; BINDING SITES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; HUMANS; LIVER; MODELS, CHEMICAL; MUTAGENESIS; OXIDATION-REDUCTION; PLACENTA; PROTEIN BINDING; RATS; SELENIUM; SELENOCYSTEINE; SPECTROPHOTOMETRY; SULFUR; THIOREDOXIN REDUCTASE (NADPH); TIME FACTORS;

ESCHERICHIA COLI; MAMMALIA;

EID: 0034646457     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.050579797     Document Type: Article

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