Magnetic Circular Dichroism of Binuclear Cobalt Complexes and Proteins

双核钴配合物和蛋白质的磁性圆二色性

• 批准号: 9708193
• 负责人: James Larrabee
• 金额: $ 10万
• 依托单位: Middlebury College
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-05-15 至 2000-04-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9708193&HistoricalAwards=false
• 关键词: Magnetic; Circular; Dichroism; Binuclear; Cobalt

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.

该无机、生物无机和有机金属化学项目奖项支持米德尔伯里学院 James A. Larrabee 博士实验室在本科院校研究 (RUI) 计划下的研究。 Larrabee 博士的研究小组将研究耦合双核钴配合物作为甲硫氨酸氨基肽酶 (MAP) 活性位点的模型。 变温变场磁圆二色性（MCD）将用于探测这种最近发现的酶的基态电子结构。 将确定模型化合物和蛋白质系统的零场分裂和磁交换常数。 由于底物分子可以跨钴离子结合，因此金属-金属交换偶联的变化对于酶的功能可能很重要。 新发现的酶——甲硫氨酸氨基肽酶中一个不寻常的钴-钴活性位点将通过磁性圆二色性进行探测。 这些光谱研究将在模型化合物和其他蛋白质上进行，这些蛋白质具有双核钴位点。 将模型化合物、理论模型和实际酶之间进行比较，以了解酶中活性位点的功能。