RAMAN STUDIES OF MEMBRANE ELECTRON TRANSFER COMPLEXES

原生的和也经过基因改变的结构和功能 (突变体)来自光合细菌的膜结合复合体 球形红杆菌，其中包括反应中心、细胞色素 Bc1(Bc1)和细胞色素c2，以及分离的发色团 在这个项目中进行了调查。时间分辨共振，表面增强 共振、傅立叶变换、非线性和紫外共振拉曼光谱 用来研究这些系统。总而言之，这些技术将提供 高灵敏度和选择性的光谱方法，可以产生 关于动力学的补充结构信息 功能。为了对光合膜进行适当的建模，请并行 模拟脂质-蛋白质体系将由单层构建 技巧。 时间分辨共振拉曼将提供有关 生色团和蛋白质结构变化的动态变化 它们的功能。将发展紫外共振拉曼光谱 用于膜复合体以确定蛋白质的性质 环境中，蛋白质组分的局部结构变化 这些复合体和蛋白质-生色团的相互作用。FT拉曼将成为 用于获得分子的非共振和共振拉曼光谱 红外区的生色团及其中间体。非线性拉曼 将尝试获取附加振动信息，该信息 在正常的拉曼散射中是不可用的。 野生型色素-蛋白质复合体及分离得到的复合体 化学诱导、自发或定点突变菌株将被 调查过了。光谱性质将在溶液中测量，并 金属表面的表面增强拉曼散射(SERS) 技巧。表面增强拉曼光谱和表面增强共振拉曼散射 (SerRS)光谱将被用来探测蛋白质的地形 膜表面并监测充电过程中发生的变化 转移到反应中心。模型的光谱研究 由Langmuir-Blodgett转移的天然单层组成的体系 和突变复合体，也是由脂质或合成聚合物稳定的 并被吸附在表面增强拉曼散射活性表面上，对于详细的 拓扑表征。

The structure and function of the native and also genetically altered (mutants) membrane-bound complexes from the photosynthetic bacterium Rhodobacter sphaeroides, which includes the reaction center, cytochrome bc1 (BC1), and cytochrome c2, as well as isolated chromophores will be investigated in this project. Time resolved resonance, surface-enhanced resonance, FT, nonlinear and UV-resonance Raman spectroscopy will be used to study these systems. Together, these techniques will provide highly sensitive and selective spectroscopic approaches that can yield complementary structural information concerning the dynamics of function. For adequate modeling of photosynthetic membranes, parallel mimetic lipid-protein systems will be constructed by monolayer techniques. Time resolved resonance Raman will provide information regarding the dynamics of structural changes in the chromophores and proteins during their functioning. UV resonance Raman spectroscopy will be developed for membrane complexes in order to establish the nature of the protein environment, the local structural changes in the protein component of these complexes and protein-chromophore interactions. FT Raman will be used to obtain nonresonance and resonance Raman spectra of the chromophores and their intermediates in the IR region. Nonlinear Raman will be attempted for obtaining additional vibrational information which is not available from normal Raman scattering. Wild-type pigment-protein complexes and complexes isolated from chemically induced, spontaneous or site-directed mutant strains will be investigated. The spectral properties will be measured in solution and at metal surfaces using surface-enhanced Raman scattering (SERS) techniques. SERS and surface-enhanced resonance Raman scattering (SERRS) spectra will be used to probe the protein topography of the membrane surface and to monitor changes that occur during charge transfer in the reaction center. Spectroscopic investigations of model systems, comprising Langmuir-Blodgett transferred monolayers of native and mutant complexes, also stabilized by lipids or synthetic polymers and absorbed on the SERS-active surfaces, will be essential for detailed topological characterization.