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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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Article information


Submitted
07 Oct 2005
Accepted
18 Nov 2005
First published
14 Dec 2005

Chem. Commun., 2006, 532-534
Article type
Communication

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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