The Interactions and Exchanges of Metal-bound Sulfur Containing Ligands with Various Transition Metals

The treble clef binding motif of the zinc finger metalloprotein utilizes N2S2 binding sites. Whereas other N2S2 metalloproteins function in catalytic roles, zinc fingers serve mostly a structural element, although there has been some evidence that the zinc finger protein can interact with exogenous metal ions in aggregate formation or ion exchange. The work presented within has been aimed at precedents for both of the latter in Zn2+. The use of zinc and cadmium dithiolate complexes as mono- and bidentate S-donor ligands to tungsten carbonyl complexes was explored and the ability of zinc and cadmium complexes to stably bind to W(CO)x (x = 4 and 5) was established. The reactivity of thiolate sulfurs within the bimetallic complexes was examined, gaining an understanding of zinc and cadmium N2S2. The characteristics of these complexes were examined via IR, UV-vis, elemental analysis, and x-ray crystallography spectroscopy. The ability of zinc to act as a scaffold for the synthesis of bisacetylbme-dach in the production and subsequent transfer of the same ligand to exogenous metal ion sources was investigated. Cu2+ and Cd2+ analogs to the Zn-1?-Ac2 were synthesized and their properties investigated with IR, elemental analysis, and UV-vis spectroscopy.