NMR STUDIES OF RESPIRATORY PROTEINS AND MODEL SYSTEMS

光谱参数的量子化学计算将是 与实验光谱学(核磁共振、红外光谱和穆斯堡尔谱)的比较 血红素蛋白的位置结构，目的是探索血红素-配体的键角 以及血红素的褶皱，特别是在顺磁状态下。长期目标 是(1)了解与血红素蛋白结合的小分子的特异性， 以及(2)验证计算核磁共振位移的量子化学方法，其他 金属蛋白质中的光谱量和能量学。关于血红素的研究 提出了蛋白质及其模型体系，包括蛋白质的密度泛函计算。 顺磁位移和穆斯堡尔分裂。各种核磁共振测量 将用于提纯肌红蛋白、一氧化碳-肌红蛋白的结构， 细胞色素c来源于铁细胞色素c-细胞色素c过氧化物酶复合体。 最后，借助对光谱血红素系统的理解，以及 有了奥德菲尔德博士精致的蛋白质结构， 小分子与亚铁血红素的结合将被研究，他假设是 以空腔内的氢键相互作用为主。

Quantum chemistry calculations of spectral parameters would be compared with experimental spectroscopy (NMR, IR and Mossbauer) on the active site structures of heme proteins, with the aim to probe heme-ligand bond angles and heme ruffling, particularly in the paramagnetic states. The long term goals are (1) to understand specificity in small molecule binding to heme proteins, and (2) to validate quantum chemical methods for computing NMR shifts, other spectroscopic quantities and energetics in metallo-proteins. Studies of heme proteins and model systems are proposed, including DFT calculations of paramagnetic shifts and Mossbauer splittings. A variety of NMR measurements will be used to refine the structures of myoglobin, carbonmonoxy-myglobin, cytochrome c from the ferricytochrome c-cytochrome c peroxidase complex. Finally, with the help of the understandng of spectroscopy heme systems, and with Dr. Oldfield's refined structures of the proteins, the energetics of binding of small molecules to hemes will be studied, which he hypothesizes are dominated by hydrogen bonding interactions in the cavity.