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FEBS Lett. 2000 Feb 11;467(2-3):221-5.

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

Author information

1
Fachrichtung 12.4 Biochemie, Universität des Saarlandes, D-66041, Saarbrücken, Germany.

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.

PMID:
10675542
DOI:
10.1016/s0014-5793(00)01102-9
[Indexed for MEDLINE]
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