TIME RESOLVED STUDIES OF HEME PROTEINS

这项研究将把时间分辨拉曼技术的应用扩展到 研究与配基结合有关的分子动力学， 多中心血红素蛋白的电子转移和催化活性 和蛋白质复合体。因此，它处于初始的 这些技术的发展及其在综合体中的应用 生物有机体的异质系统。 细胞色素氧化酶、细胞色素c过氧化物酶、细胞色素c复合体和bc1 已经选择了络合物进行研究，并进行了合作 与隔离和准备这些系统的专家一起启动。 这些蛋白质表现出各种催化和电子转移。 可通过特定协议光启动的功能。详细的 共振拉曼光谱的结构信息将提供 适当时间的相关机械数据-分辨率(PSEC至毫秒)。 将使用低温研究来确定激活 这些过程的能量学。瞬变拉曼差分技术将 为了将贡献与个人氧化还原分离出来而开发 在功能过程中的中心。

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.