Metal Cluster Active Sites in Proteins

Que博士将研究氯氰菊酯、紫色酸性磷酸和甲烷单加氧酶的活性中心结构，以及在原型甲基氯氰菊酯活性中心发现的氧桥联双核簇在这组蛋白质中的保守程度。用核磁共振、EXFAS、EPR、穆斯堡尔谱、磁化率和共振拉曼光谱等技术对活性中心进行了研究。必要时将使用模型化合物来确定光谱特征。在活性部位含有铁氧簇的蛋白质构成了金属蛋白的一个亚类，包括杂氰菊酯、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。杂草菊酯在海洋无脊椎动物中作为氧运输蛋白发挥作用。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的水解，而甲烷单加氧酶将甲烷转化为甲醇。奎博士将研究大自然如何调整星团的环境，以执行这些不同的生化反应。

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.