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

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

Volumn 97, Issue 11, 2000, Pages 5854-5859

  Zhong, Liangwei ^a   Arnér, Elias S J ^a   Holmgren, Arne ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Disulfide; Enzyme structure; Evolution; Selenium; Thiols

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; AUROTHIOGLUCOSE; CYSTEINE DERIVATIVE; DITHIOL DERIVATIVE; GLUTATHIONE REDUCTASE; HYDROPEROXIDE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SELENOCYSTEINE; THIOREDOXIN REDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; MASS SPECTROMETRY; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RAT;

ANIMALS; BINDING SITES; CATTLE; CYSTEINE; GLUTATHIONE REDUCTASE; MASS SPECTROMETRY; MODELS, MOLECULAR; NADP; OXIDATION-REDUCTION; SELENOCYSTEINE; THIOREDOXIN REDUCTASE (NADPH);

EID: 0034705133     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.100114897     Document Type: Article

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