High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron

Proteins: Structure, Function and Genetics

Volumn 50, Issue 2, 2003, Pages 261-271

  Andreoletti, Pierre ^a   Sainz, Germaine ^b   Jaquinod, Michel ^c   Gagnon, Jean ^a   Jouve, Hélène Marie ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^c Caprion Pharmaceuticals   (Canada)

Author keywords

Methionine sulfone; Protoporphyrin IX; Recombinant Proteus mirabilis catalase; X ray crystallography

Indexed keywords

CATALASE; HISTIDINE; IRON; PROTOPORPHYRIN; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAMER;

ARTICLE; BIOCHEMISTRY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE OVEREXPRESSION; HYDROGEN BOND; IRON DEPLETION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEUS MIRABILIS;

ACETATES; ANIONS; ARGININE; BINDING SITES; CATALASE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HEME; HYDROGEN BONDING; IRON; MODELS, MOLECULAR; NADP; PROTEIN CONFORMATION; PROTEUS MIRABILIS; PROTOPORPHYRINS; RECOMBINANT PROTEINS; SPECTRUM ANALYSIS; SULFATES;

MIRABILIS; PROTEUS MIRABILIS;

EID: 0037297450     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10283     Document Type: Article

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