Spectroscopic and Magnetic Studies of Metalloprotein Active Sites

金属蛋白活性位点的光谱和磁学研究

• 批准号: 9019752
• 负责人: Edward Solomon
• 金额: $ 28.59万
• 依托单位: Stanford University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1991
• 资助国家: 美国
• 起止时间: 1991-03-01 至 1994-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9019752&HistoricalAwards=false
• 关键词: Spectroscopic; Magnetic; Studies; Metalloprotein; Active

A coupled binuclear non-heme iron active site exists in a variety of proteins which perform different biological functions. hemerythrin (Hr) binds O2, methane monooxygenase activates it for hydroxylation, reducted ribonucleotide reductase reacts with O2 to generate a catalytically active tyrosyl radical, and reduced purple acid phosphatase is oxidatively inactivated in the presence of phosphate. These protein sites (and analogous model complexes) can be obtained in three oxidation states. Dr. Solomon's spectral studies on these sites and their substrate and small molecule bound forms emphasize bsorption, circular dichrosims, and magnetic circular dichroism (MCD) to probe the excited states, and variable- temperature, variable-field MCD to probe ground state sublevel splittings. This data enables a determination of the geometry of each iron, and the exchange coupling which is associated with bridging ligation. The goal of this research is to define active site geometric and electronic structural diffeences which correlate with variation in biological reactivity.

一个耦合的双核非血红素铁活性中心存在于一个 各种蛋白质，它们执行不同的生物学功能， 功能协调发展的 血红蛋白（Hr）结合O2、甲烷单加氧酶 激活它进行羟基化， 还原酶与O2反应， 酪氨酰自由基和还原的紫色酸性磷酸酶是 在磷酸盐存在下氧化失活。 这些 可以获得蛋白质位点（和类似的模型复合物 三种氧化态。 所罗门博士的光谱研究 这些位点及其底物和小分子结合形式 强调吸收、圆二色性和磁性圆二色性 二向色性（MCD）探测激发态，和可变- 探测基态次能级温度、变场MCD 分裂 该数据使得能够确定几何形状 每一个铁，和交换耦合是相关联的 用桥接连接。 这项研究的目的是确定 活性位几何结构和电子结构的有序性 其与生物反应性的变化相关。