HEME-PROTEIN DYNAMICS IN MULTI-CENTER SYSTEMS

本研究将扩大时间分辨拉曼光谱的应用范围 分子动力学研究中的技术问题 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质复合体的活性。 因此，它处于初始开发的交界处 这些技术及其在综合体中的应用 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 选择了络合物和Bc1络合物作为研究对象，并 已经开始与隔离中的专家进行合作 以及这些系统的准备。这些蛋白质表现出 各种催化和电子转移函数，可能是 通过特定协议启动的照片。细部结构 共振拉曼光谱的信息将提供 适当时间的相关机械数据-分辨率(PSEC至 毫秒)。将利用低温研究来确定 这些过程的活化能量学。瞬变拉曼 将开发不同的技术来分离 来自各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.