Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction

Journal of Biological Chemistry

Volumn 274, Issue 51, 1999, Pages 36039-36042

  Shi, Jin ^a   Vlamis Gardikas, Alexios ^b   Åslund, Fredrik ^b   Holmgren, Arne ^b   Rosen, Barry P ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC ACID; GLUTAREDOXIN 1; GLUTAREDOXIN 2; GLUTAREDOXIN 3; GLUTATHIONE DISULFIDE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DISULFIDE BOND; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ARSENATES; ARSENITES; BACTERIAL PROTEINS; ELECTRON TRANSPORT; ESCHERICHIA COLI; HYDROGEN; OXIDOREDUCTASES; PROTEINS;

ANIMALIA; ESCHERICHIA COLI;

EID: 0033579499     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.51.36039     Document Type: Article

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