Metal Cluster Active Sites in Proteins

蛋白质中的金属簇活性位点

• 批准号: 8804458
• 负责人: Lawrence Que
• 金额: $ 24万
• 依托单位: University of Minnesota-Twin Cities
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-08-01 至 1992-01-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8804458&HistoricalAwards=false
• 关键词: Metal; Cluster; Active; Sites; Proteins

Dr. Que will investigate the active site structures of hemerythrin, purple acid phosphates and methane monooxygenase and the extent that the oxo.bridged binuclear clusters found in the prototypical methemerythrin active site is conserved in this group of proteins. NMR, EXFAS, EPR, Mossbauer, magnetic susceptibility and resonance Raman techniques will be applied to study the active sites. Model compounds will be used as necessary to ascertain spectroscopic signatures. Proteins containing iron.oxo clusters at their active sites constitute a subclass of metalloproteins which include hemerythrin, certain ribonucleotide reductases, purple acid phosphatases possibly methane monooxygenase. The hemerythrins function as oxygen transport proteins in marine invertebrates. The ribonucleotide reductases convert ribonucleotides to deoxyribonucleotides and are therefore important for cell replication. The purple acid phosphatases catalyze the hydrolysis of phosphate esters while methane monooxygenase converts methane to methanol. Dr. Que will investigate how nature can tune the environment of the cluster to perform these different biochemical reactions.

柯博士将研究菊氰菊酯、紫色酸性磷酸酯和甲烷单加氧酶的活性位点结构，以及氧合酶的作用程度。在甲基菊酯活性位点的桥接双核簇在这组蛋白中是保守的。将应用核磁共振、EXFAS、EPR、穆斯堡尔、磁化率和共振拉曼等技术对活性位点进行研究。必要时将使用模型化合物来确定光谱特征。含铁的蛋白质活性位点上的氧簇构成了金属蛋白的一个亚类，包括氰菊酯、某些核糖核苷酸还原酶、紫色酸性磷酸酶（可能是甲烷单加氧酶）。氰菊酯在海洋无脊椎动物中起氧转运蛋白的作用。核糖核苷酸还原酶将核糖核苷酸转化为脱氧核糖核苷酸，因此对细胞复制很重要。紫色酸性磷酸酶催化磷酸酯水解，而甲烷单加氧酶将甲烷转化为甲醇。Que博士将研究大自然如何调节集群的环境来执行这些不同的生化反应。