Kinetic and spectroscopic characterization of native and metal‐substituted β‐lactamase from Aeromonas hydrophila AE036
- 7 February 2000
- journal article
- Published by Wiley in FEBS Letters
- Vol. 467 (2-3) , 221-225
- https://doi.org/10.1016/s0014-5793(00)01102-9
Abstract
Two metal ion binding sites are conserved in metallo‐β‐lactamase from Aeromonas hydrophila. The ligands of a first zinc ion bound with picomolar dissociation constant were identified by EXAFS spectroscopy as one Cys, two His and one additional N/O donor. Sulfur‐to‐metal charge transfer bands are observed for all mono‐ and di‐metal species substituted with Cu(II) or Co(II) due to ligation of the single conserved cysteine residue. Binding of a second metal ion results in non‐competitive inhibition which might be explained by an alternative kinetic mechanism. A possible partition of metal ions between the two binding sites is discussed.Keywords
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