Zinc is essential to all forms of life and is the second most abundant trace element in the human body. Correspondingly, zinc participates in a wide variety of biological processes, which include carbohydrate, lipid, protein and nucleic acid synthesis, regulation, and degradation. Zinc is, therefore, an indispensable element for effective growth and development, with deficiency resulting in organ malformations. In order to be able to understand fully the consequences of zinc deficiency, and hence suggest possible remedies, it is most essential to understand the bioinorganic chemistry of zinc. The aim of this proposal is to define more fully the bioinorganic chemistry of zinc with respect to a selection of zinc enzymes, which include carbonic anhydrase, carboxypeptidase, thermolysis and liver alcohol dehydrogenase. Specifically, the bioinorganic chemistry of zinc will be delineated by studying the chemistry of synthetic analogs, i.e. simple molecules that are intended to mimic both the structure and function of the active sites of zinc enzymes. Synthetic analogs are more amenable to structural, spectroscopic, and mechanistic studies than the enzymes themselves, so that definitive investigations of these systems will allow considerable insight into the mechanism of action of the enzymes to be ascertained. The results of these studies could significantly improve our understanding of the bioinorganic chemistry of zinc and consequently could be of considerable importance in providing a rational basis of curing diseases resulting from zinc deficiency.