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

锡拉丘兹大学的Laurence A. Nafie博士的小非手性配体作为金属蛋白活性位点的振动圆二色性（VCD）探针的研究获得了化学学部物理化学项目的资助。改进的实验测量和理论计算将用于完成VCD作为金属蛋白中金属配体活性位点的敏感探针的开发。将获得有关金属蛋白配合物溶液态结构和构象的新信息，并对(1)相关金属中心的低洼电子结构，(2)金属蛋白中的蛋白质袋环境，以及(3)这些结构元素与VCD光谱中观察到的振动模式的耦合获得新的见解。这些研究将积极影响相关的振动测量技术，如金属蛋白复合物中的红外吸收和共振拉曼散射。利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。锡拉丘兹大学金属蛋白及其相关复合物的振动圆二色性研究将扩展我们对金属蛋白的结构-功能理解，金属蛋白对生物系统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.