Human cytoplasmic aconitase (iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding

Journal of Biological Chemistry

Volumn 274, Issue 31, 1999, Pages 21625-21630

  Brazzolotto, Xavier ^a   Gaillard, Jacques ^b   Pantopoulos, Kostas ^c,d   Hentze, Matthias W ^c   Moulist, Jean Marc ^a  

^a Dept de Biol Molec et Structurale   (France)

^b Europ Molecular Biology Laboratory ^*  (France)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^d MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; HYDROGEN PEROXIDE; IRON REGULATORY FACTOR;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; HOMEOSTASIS; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN SYNTHESIS REGULATION; RNA BINDING;

ACONITATE HYDRATASE; CYCLIC N-OXIDES; CYTOPLASM; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; HYDROGEN PEROXIDE; IRON REGULATORY PROTEIN 1; IRON-REGULATORY PROTEINS; IRON-SULFUR PROTEINS; KINETICS; RECOMBINANT PROTEINS; RNA, MESSENGER; RNA-BINDING PROTEINS; SPIN LABELS; SUBSTRATE SPECIFICITY; SUPEROXIDES;

EID: 0033618254     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.31.21625     Document Type: Article

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