Thioredoxin reductase: Two modes of catalysis have evolved

European Journal of Biochemistry

Volumn 267, Issue 20, 2000, Pages 6110-6117

  Williams Jr , Charles H ^a,b   David Arscott, L ^a   Müller, Sylke ^b,c   Lennon, Brett W ^d   Ludwig, Martha L ^b,d   Wang, Pan Fen ^b   Veine, Donna M ^a   Becker, Katja ^e,f   Heiner Schirmer, R ^e  

^a VA ANN ARBOR HEALTHCARE SYSTEM   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c BERNHARD NOCHT INSTITUTE FOR TROPICAL MEDICINE   (Germany)

^d UNIVERSITY OF MICHIGAN   (United States)

^e UNIVERSITY OF HEIDELBERG   (Germany)

^f UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

Disulfide; Dithiol; Drug design; Flavoprotein; Redox active; Ribonucleotide reductase; Selenenylsulfide; Selenium; Thioredoxin; Thioredoxin reductase; Transcription factor activation

Indexed keywords

DISULFIDE; DITHIOL DERIVATIVE; FLAVOPROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RIBONUCLEOTIDE REDUCTASE; SELENIUM; THIOREDOXIN; THIOREDOXIN REDUCTASE; TRANSCRIPTION FACTOR;

CATALYSIS; CONFORMATIONAL TRANSITION; DRUG DESIGN; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; MALARIA; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; NONHUMAN; OXIDATION REDUCTION REACTION; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN FAMILY; SHORT SURVEY;

ANIMALS; CATALYSIS; ESCHERICHIA COLI; HUMANS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; THIOREDOXIN REDUCTASE (NADPH);

EID: 0033781942     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01702.x     Document Type: Short Survey

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