TIME RESOLVED STUDIES OF HEME PROTEINS

这项研究将扩展时间分辨拉曼技术的应用， 与配体结合相关的分子动力学研究， 多中心血红素蛋白的电子转移和催化活性 和蛋白质复合物。 因此，它位于初始 这些技术的发展及其在复杂的应用 生物体的异质系统。 细胞色素氧化酶、细胞色素c过氧化物酶、细胞色素c复合物和bc1 复合体已被选择进行研究，合作已被 在隔离和准备这些系统方面与专家一起发起。 这些蛋白质表现出多种催化和电子转移 可以通过特定的方案光引发的功能。 的详细 共振拉曼光谱结构信息将提供 适当时间分辨率（psec至msec）的相关机械数据。 将采用低温研究来确定活化 这些过程的能量学。 瞬态拉曼差分技术将 开发，以隔离贡献，从个人的氧化还原 在功能过程中。

This study will extend the application of time-resolved Raman techniques to the investigation of the molecular dynamics associated with ligand binding, electron transfer, and catalytic activities of multicenter heme proteins and protein complexes. It is thus at the interface between the initial development of these techniques and their application to the complex heterogeneous systems of living organisms. Cytochrome oxidase, cytochrome c peroxidase.cytochrome c complexes, and bc1 complexes have been chosen for study, and collaborations have been initiated with experts in the isolation and preparation of those systems. These proteins exhibit a variety of catalytic and electron transfer functions that may be photoinitiated via specific protocols. The detailed structural information of resonance Raman spectroscopy will provide relevant mechanistic data at appropriate time-resolution (psec to msec). Low temperature studies will be employed to determine the activation energetics of those processes. Transient Raman difference techniques will be developed in order to isolate contributions from individual redox centers during functional processes.