Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond

FEBS Letters

Volumn 449, Issue 2-3, 1999, Pages 196-200

  Nordstrand, Kerstin ^a   Åslund, Fredrik ^a   Meunier, Sylvie ^a   Holmgren, Arne ^a   Otting, Gottfried ^a   Berndt, Kurt D ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Enzyme mechanism; Glutaredoxin; Thiol pK(a)

Indexed keywords

CYSTEINE; GLUTAREDOXIN 3; OXIDOREDUCTASE; THIOREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN BINDING;

BACTERIAL PROTEINS; BINDING SITES; CYSTEINE; ESCHERICHIA COLI; HYDROGEN BONDING; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEINS; PROTONS; SULFHYDRYL COMPOUNDS;

ESCHERICHIA COLI;

EID: 0032959801     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)00401-9     Document Type: Article

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