Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria

Journal of Biological Chemistry

Volumn 282, Issue 5, 2007, Pages 3077-3082

  Johansson, Catrine ^a   Kavanagh, Kathryn L ^a   Gileadi, Opher ^a   Oppermann, Udo ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HUMAN MITOCHONDRIAL GLUTAREDOXIN 2 (GLRX2); MITOCHONDRIA; POLAR INTERACTION;

CELL DEATH; DIMERS; ENZYME INHIBITION; MONOMERS; OXIDATIVE STRESS;

AMINO ACIDS;

CYSTEINE; DIMER; GLUTAREDOXIN; GLUTAREDOXIN 2; GLUTATHIONE; IRON; MITOCHONDRIAL PROTEIN; MONOMER; SULFUR; UNCLASSIFIED DRUG; GLUTATHIONE DISULFIDE; IRON SULFUR PROTEIN; ISOENZYME; OXIDOREDUCTASE; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; MITOCHONDRIAL RESPIRATION; MITOCHONDRION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; CRYSTALLIZATION; DIMERIZATION; ENZYMOLOGY; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GLUTATHIONE; GLUTATHIONE DISULFIDE; HUMANS; IRON-SULFUR PROTEINS; ISOENZYMES; MITOCHONDRIA; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 34047250626     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M608179200     Document Type: Article

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