Phosphatases are an integral enzyme for cellular signal transduction. These enzymes are able to remove a highly charged phosphate from other enzymes changing their configuration and thus causing them to either become active or inactive. Over the past few decades, many crystal structures of phosphatases have been determined with vanadium and some vanadium complexes bound in the active site. Using data mining through the protein database, we looked at vanadium-phosphatase complexes and found that vanadium prefers the trigonal bipyramidal geometry over the square pyramidal geometry. The efficacies of vanadium-based inhibitors such as vanadium complexes and oxometalates, were also evaluated to discuss inhibitor design. In all cases involving vanadium complexes but one, the vanadium was found bound to the active site of the phosphatase most likely due to experimental conditions and hydrolysis of the vanadium complex. The Ki across many phosphatases were also examined and no matter the initial geometry of the vanadium complex, the Ki value only spanned three orders of magnitude1. 1. C. C. McLauchlan, B. J. Peters, G. R. Willsky and D. C. Crans, Coordination Chemistry Reviews, DOI: http://dx.doi.org/10.1016/j.ccr.2014.12.012.

Vanadium phosphatase inhibitors favor the trigonal bipyramidal transition state geometry

250th National Meeting (2015)

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