Small Achiral Ligands as Vibrational Circular Dichroism Probes of Active Sites in Metalloproteins

锡拉丘兹大学的Laurence A.Nafie博士因其作为金属蛋白质活性中心的振动圆二色(VCD)探针的小非手性配体的研究而获得化学系物理化学计划的资助。改进的实验测量和理论计算将被用来完成VCD作为金属蛋白中金属配体活性中心的灵敏探针的发展。将产生有关金属蛋白络合物的溶液状态结构和构象的新信息，并将获得对(1)相关金属中心的低位电子结构，(2)金属蛋白中的蛋白质口袋环境，以及(3)这些结构元素与在VCD光谱中观察到的振动模式的耦合的新的见解。这些研究将对相关的振动测量技术产生积极的影响，如金属蛋白络合物的红外吸收和共振拉曼散射。使用各种光谱来更好地了解蛋白质的结构和功能是实验物理化学的长期目标。锡拉丘兹大学对金属蛋白及其相关络合物的振动圆二色谱研究将扩大我们对金属蛋白的结构和功能的了解，金属蛋白对生物系统中的能量代谢非常重要。

Dr. Laurence A. Nafie of Syracuse University is funded for his research on small achiral ligands as vibrational circular dichroism (VCD) probes of active sites in metalloproteins by the Physical Chemistry Program of the Chemistry Division. Improved experimental measurements and theoretical calculations will be used to complete the developement of VCD as a sensitive probe of metal-ligand active-sites in metalloproteins. New information about the solution-state structure and conformaton of metalloprotein complexes will be generated, and new insight into the (1) low-lying electronic structure of associated metal centers, (2) protein pocket environments in metalloproteins, and (3) coupling of these structural elements to the vibrational modes observed in VCD spectra will be obtained. Such studies will positively impact associated vibrational measurement techniques such as IR absorption and resonance Raman scattering in metalloprotein complexes.The use of various spectroscopies to better understand protein structure and function is a long-standing goal of experimental physical chemistry. The vibrational circular dichroism studies of metalloproteins and associated complexes at Syracuse University will extend our structure-function understanding of metalloproteins, so important to energy metabolism in biological systems.