Magnetic Circular Dichroism of Binuclear Cobalt Complexes and Proteins

该奖项属于无机、生物无机和有机金属化学项目，支持米德尔伯里学院詹姆斯·a·拉拉比博士在本科院校研究（RUI）计划下的实验室研究。Larrabee博士的研究小组将研究偶联双核钴配合物作为蛋氨酸氨基肽酶（MAP）活性位点的模型。变温变场磁圆二色性（MCD）将被用来探测这种新发现的酶的基态电子结构。将确定模型化合物和蛋白质体系的零场分裂常数和磁交换常数。由于底物分子可以通过钴离子结合，金属-金属交换偶联的变化可能对酶的功能很重要。一种新发现的酶——蛋氨酸氨基肽酶中一个不寻常的钴-钴活性位点将通过磁圆二色性进行探测。这些光谱研究将在模型化合物和其他蛋白质上进行，这些蛋白质中有一个双核钴位点被取代。将模型化合物、理论模型和实际酶进行比较，以了解酶活性位点的功能。

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.