Magnetic Circular Dichroism of Binuclear Cobalt Complexes and Proteins

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This award in the Inorganic, Bioinorganic and Organometallic chemistry program supports research in the laboratory of Dr. James A. Larrabee at Middlebury College under the Research in Undergraduate Institutions (RUI) initiative. Dr. Larrabee's research group will investigate coupled binuclear cobalt complexes as models for the active site in methionine amino peptidase (MAP). Variable-temperature, variable-field magnetic circular dichroism (MCD) will be used to probe the ground state electronic structure of this recently discovered enzyme. Zero-field splitting and magnetic exchange constants will be determined for model compounds and protein systems. Since substrate molecules may bind across the cobalt ions, changes in metal-metal exchange coupling may be important in the functioning of the enzyme. An unusual cobalt-cobalt active site in a newly discovered enzyme, methionine amino peptidase, will be probed by magnetic circular dichroism. These spectroscopic studies will be carried on model compounds and other proteins, which have a dinuclear cobalt site substituted into them. Comparisons between the model compounds, theoretical models and the actual enzyme will be made in order to understand the functioning of the active site in the enzyme.