Positively Cooperative Binding of Zinc Ions to Bacillus cereus 569/H/9 β-Lactamase II Suggests that the Binuclear Enzyme Is the Only Relevant Form for Catalysis

Journal of Molecular Biology

Volumn 392, Issue 5, 2009, Pages 1278-1291

  Jacquin, Olivier ^a   Balbeur, Dorothée ^a   Damblon, Christian ^b   Marchot, Pierre ^a   De Pauw, Edwin ^a   Roberts, Gordon C K ^b   Frère, Jean Marie ^a   Matagne, André ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

circular dichroism; cooperativity; mass spectrometry; metallo lactamases; NMR

Indexed keywords

APOENZYME; CADMIUM; CEPHALOSPORINASE; CHELATING AGENT; FURAPTRA; ZINC ION;

ALPHA HELIX; ARTICLE; BACILLUS CEREUS; CATALYSIS; CHROMATOPHORE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; MASS SPECTROMETRY; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; ULTRAVIOLET RADIATION;

BACILLUS CEREUS;

ANTI-BACTERIAL AGENTS; BACILLUS CEREUS; BACTERIAL PROTEINS; BETA-LACTAMASES; BETA-LACTAMS; CIRCULAR DICHROISM; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; PROTEIN BINDING; SPECTROPHOTOMETRY; ZINC;

EID: 70249131429     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.092     Document Type: Article

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