Abstract
Abstract To model substrate binding to zinc containing enzymes, Zn(Tp∗)Cl (Tp∗ = tris(3,5-dimethyl-1-pyrazolyl)borate) was investigated as an inexpensive and easily prepared target. Both acetyl hydroxamic acid and acetic acid, common zinc binding moieties, were found to bind zinc in our model system and the resulting complexes were fully characterized. The hydroxamate complex was found to be both thermodynamically and kinetically favored in comparison to the acetate complex, in keeping with previous models, demonstrating the utility of this system in enzymatic mimicry.
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