13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins

European Journal of Biochemistry

Volumn 271, Issue 8, 2004, Pages 1437-1452

  Eisenreich, Wolfgang ^a   Kemter, Kristina ^a   Bacher, Adelbert ^a   Mulrooney, Scott B ^b,e   Williams Jr , Charles H ^b,c   Müller, Franz ^d  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c VA ANN ARBOR HEALTHCARE SYSTEM   (United States)

^d Michigan State University ^*  (Switzerland)

^e MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

FAD; Flavin apoprotein interaction; Flavoprotein; NMR spectroscopy; Thioredoxin reductase

Indexed keywords

APOPROTEIN; ENZYME; FLAVOPROTEIN; HYDROGEN; MUTANT PROTEIN; PHENYLMERCURIC ACETATE; PROTEIN; QUERCETIN; THIOREDOXIN REDUCTASE; CARBON; FLAVINE ADENINE NUCLEOTIDE; NITROGEN; OXIDOREDUCTASE; PHOSPHORUS; RECOMBINANT PROTEIN; RIBOFLAVIN DERIVATIVE;

ARTICLE; ATOM; CARBON NUCLEAR MAGNETIC RESONANCE; ENZYME METABOLISM; HYDROGEN BOND; INTERMETHOD COMPARISON; MOLECULAR INTERACTION; MOLECULAR WEIGHT; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; REDUCTION; X RAY; AMINO ACID SUBSTITUTION; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; METHODOLOGY; MUTATION; OXIDATION REDUCTION REACTION; ULTRAVIOLET SPECTROPHOTOMETRY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

AMINO ACID SUBSTITUTION; CARBON ISOTOPES; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; FLAVINS; MOLECULAR WEIGHT; MUTATION; NADH, NADPH OXIDOREDUCTASES; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PHOSPHORUS ISOTOPES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; THIOREDOXIN REDUCTASE (NADPH);

EID: 2142642259     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04043.x     Document Type: Article

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