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. Copyright (C) 2000 Federation of European Biochemical Societies.
|Titolo:||Kinetic and spectroscopic characterization of native and metal-substituted β-lactamase from Aeromonas hydrophila AE036|
|Autori interni:||AMICOSANTE, Gianfranco|
|Data di pubblicazione:||2000|
|Appare nelle tipologie:||1.1 Articolo in rivista|