68 Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase
Chemical communications, 2006•pubs.rsc.org
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.
(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.
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.
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