HEME-PROTEIN DYNAMICS IN MULTI-CENTER SYSTEMS

本研究将扩展时间分辨拉曼光谱的应用范围 分子动力学研究的新技术 与配体结合、电子转移和催化有关 多中心血红素蛋白和蛋白复合物的活性。 因此，它处于初始发展与 这些技术及其在复合体中的应用 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 配合物和bc1配合物已被选择用于研究， 已经开始与隔离区的专家合作， 这些系统的准备。 这些蛋白质表现出 各种催化和电子转移功能， 通过特定的协议进行光引发。 详细结构 共振拉曼光谱信息将提供 适当时间分辨率下的相关机械数据（psec至 毫秒）。 将采用低温研究来确定 这些过程的活化能。 瞬态拉曼 将开发差异技术，以分离 在功能过程中，单个氧化还原中心的贡献 流程.

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 multi-center heme proteins and protein complexes. It is thus at the interface between the initial development of these techniques and their application to the complex heterogenous 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 photo-initiated 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.