Evidence for two conformational states of thioredoxin reductase from Escherichia coli: Use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation

Protein Science

Volumn 6, Issue 10, 1997, Pages 2188-2195

  Mulrooney, Scott B ^a   Williams Jr , Charles H ^a,b  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

Conformation; Cys modification; FAD fluorescence; Flavoproteins; Fluorescence quenching; Limited proteolysis; Thioredoxin reductase

Indexed keywords

QUERCETIN; THIOREDOXIN REDUCTASE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL;

EID: 0030866966     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061013     Document Type: Article

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