Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency

Journal of the American Chemical Society

Volumn 128, Issue 51, 2006, Pages 16684-16691

  Metanis, Norman ^a,b   Keinan, Ehud ^a,b   Dawson, Philip E ^b  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EXCHANGE REACTIONS; NUCLEOPHILICITY; REDOX POTENTIAL; SELENOCYSTEINE (SEC);

BIOCHEMISTRY; CATALYST ACTIVITY; CHEMICAL BONDS; REDOX REACTIONS; REDUCTION; SYNTHESIS (CHEMICAL);

ENZYMES;

DISULFIDE; GLUTAREDOXIN; OXIDOREDUCTASE; PEROXIDE; SELENATE; SELENIUM DERIVATIVE; SELENIUM SULFIDE; SELENOCYSTEINE; SELENOGLUTAREDOXIN 3 DERIVATIVE; SULFOXIDE; THIOREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL BINDING; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SYNTHESIS; EQUILIBRIUM CONSTANT; OXIDATION REDUCTION REACTION; REDUCTION KINETICS;

BINDING SITES; CATALYSIS; MOLECULAR STRUCTURE; ORGANOSELENIUM COMPOUNDS; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; TIME FACTORS;

EID: 33845940127     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0661414     Document Type: Article

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