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

Maria Hernandez Valladares, Martin Kiefer, Uwe Heinz, Raquel Paul Soto, Wolfram Meyer-Klaucke, Hans Friederich Nolting, Michael Zeppezauer, Moreno Galleni, Jean Marie Frère, Gian Maria Rossolini, Gianfranco Amicosante, Hans Werner Adolph

Research output: Contribution to journalArticlepeer-review

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. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)221-225
Number of pages5
JournalFEBS Letters
Volume467
Issue number2-3
DOIs
Publication statusPublished - Feb 11 2000

Keywords

  • EXAFS
  • Kinetics
  • Metal exchange
  • Metallo-β-lactamase
  • UV-vis spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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