Lead is a toxic environmental pollutant that can cause severe damage even in small amounts.  While the exact process by which lead poisoning occurs is not known, it is clear that lead binds to sulfur-rich sites in proteins.  This presentation will describe the characterization and reactivity of a series of nitrogen/sulfur-ligated Pb(II) compounds of relevance to biological systems.  The compounds differ in the nature of the secondary environment introduced by the supporting chelate ligand.   These changes cause shifts in the 207Pb NMR resonance as well as differences in the water coordination chemistry at the Pb(II) center.  Kinetic studies were undertaken to understand the effect of Pb(II) on amide methanolysis reactivity versus that found for a Zn(II)-containing analog. The results of this study are of relevance toward understanding how Pb(II)-substitution in zinc proteins can influence biological reactivity.

Nitrogen/sulfur-coordinated Pb(II) complexes

245th National Meeting (2013)

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