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Issue 5, 2006
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68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase

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Abstract

The apparently paradoxical behaviour of facile exchange (kinetic lability) of tightly bound (thermodynamic stability) zinc ions in the enzyme IMP-1 metallo-β-lactamase with Zn-68 and cadmium ions, as indicated by in-torch vaporization inductively-coupled plasma mass spectrometry (ITV-ICP-MS) and electrospray-ionization mass spectrometry (ESI-MS), is consistent with the involvement of a third metal ion in promoting Lewis acid/base type exchange processes.

Graphical abstract: 68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase

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Publication details

The article was received on 07 Oct 2005, accepted on 18 Nov 2005 and first published on 14 Dec 2005


Article type: Communication
DOI: 10.1039/B514227J
Citation: Chem. Commun., 2006, 532-534
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    68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase

    S. Siemann, H. R. Badiei, V. Karanassios, T. Viswanatha and G. I. Dmitrienko, Chem. Commun., 2006, 532
    DOI: 10.1039/B514227J

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