Metal Ion Binding and Coordination Geometry for Wild Type and Mutants of Metallo-β-lactamase from Bacillus cereus569/H/9 (BcII)
Open Access
- 1 November 2001
- journal article
- Published by Elsevier
- Vol. 276 (48) , 45065-45078
- https://doi.org/10.1074/jbc.m106447200
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Standard Numbering Scheme for Class B β-LactamasesAntimicrobial Agents and Chemotherapy, 2001
- Kinetic and spectroscopic characterization of native and metal‐substituted β‐lactamase from Aeromonas hydrophila AE036FEBS Letters, 2000
- Structural effects of the active site mutation cysteine to serine inBacillus cereuszinc-β-lactamaseProtein Science, 2000
- The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolution 1 1Edited by K. NagaiJournal of Molecular Biology, 1998
- Mono‐ and binuclear Zn‐β‐lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ionsFEBS Letters, 1998
- Crystal Structure of the Zinc-Dependent β-Lactamase from Bacillus cereus at 1.9 Å Resolution: Binuclear Active Site with Features of a Mononuclear Enzyme,Biochemistry, 1998
- Spectroscopic Characterization of a Binuclear Metal Site in Bacillus cereus β-Lactamase IIBiochemistry, 1998
- Zn(II) Dependence of the Aeromonas hydrophila AE036 Metallo-β-lactamase Activity and StabilityBiochemistry, 1997
- The Protein Conformation of Cd‐Substituted Horse Liver Alcohol Dehydrogenase and its Metal‐Site Coordination Geometry in Binary and Ternary Inhibitor ComplexesEuropean Journal of Biochemistry, 1996
- Some applications of statistical tests in analysis of EXAFS and SEXAFS dataJournal of Physics C: Solid State Physics, 1987