Role of the dimeric structure in Cu,Zn superoxide dismutase: pH- dependent, reversible denaturation of the monomeric enzyme from Escherichia coli

Journal of Biological Chemistry

Volumn 273, Issue 10, 1998, Pages 5655-5661

  Battistoni, Andrea ^a   Folcarelli, Silvia ^a   Cervoni, Laura ^b   Polizio, Francesca ^a   Desideri, Alexandre ^a   Giartosio, Anna ^b   Rotilio, Giuseppe ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

APOENZYME; COPPER ZINC SUPEROXIDE DISMUTASE; CYSTEINE; DIMER; EDETIC ACID; METAL ION; MONOMER; SOLVENT;

ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; METAL BINDING; NONHUMAN; PH; PRIORITY JOURNAL;

APOENZYMES; BINDING SITES; CALORIMETRY, DIFFERENTIAL SCANNING; DIMERIZATION; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SUPEROXIDE DISMUTASE; TEMPERATURE; THERMODYNAMICS; UREA;

BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; EUKARYOTA;

EID: 0032489361     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.10.5655     Document Type: Article

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