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. 2000 Feb 11;467(2-3):221-5.
doi: 10.1016/s0014-5793(00)01102-9.

Kinetic and spectroscopic characterization of native and metal-substituted beta-lactamase from Aeromonas hydrophila AE036

M Hernandez Valladares  1 , M Kiefer, U Heinz, R P Soto, W Meyer-Klaucke, H F Nolting, M Zeppezauer, M Galleni, J M Frère, G M Rossolini, G Amicosante, H W Adolph
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Free article

Kinetic and spectroscopic characterization of native and metal-substituted beta-lactamase from Aeromonas hydrophila AE036

M Hernandez Valladares et al. FEBS Lett. .
Free article

Erratum in

  • FEBS Lett 2000 Jul 21;477(3):285

Abstract

Two metal ion binding sites are conserved in metallo-beta-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.

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