RAMAN STUDIES OF MEMBRANE ELECTRON TRANSFER COMPLEXES

结构和功能的天然和基因改变 （突变体）来自光合细菌的膜结合复合物 球形红细菌，其中包括反应中心，细胞色素 bc 1（BC 1）和细胞色素c2，以及分离的发色团将被 在这个项目中进行了调查。 时间分辨共振，表面增强 共振，FT，非线性和紫外共振拉曼光谱将是 用来研究这些系统。 总之，这些技术将提供 高灵敏度和选择性的光谱方法， 关于动力学的补充结构信息 功能 为了充分模拟光合膜， 模拟脂质-蛋白质系统将通过单层构建 技术. 时间分辨共振拉曼将提供关于 发色团和蛋白质结构变化的动力学 他们的功能。 将开发紫外共振拉曼光谱 为了确定蛋白质的性质， 环境中，蛋白质组分的局部结构变化 这些复合物和蛋白质-发色团相互作用。 FT拉曼将是 用于获得非共振和共振拉曼光谱的 发色团及其中间体在IR区域。 非线性拉曼 将试图获得额外的振动信息， 不能从正常的拉曼散射中获得。 野生型色素-蛋白质复合物和分离自 化学诱导的、自发的或定点突变株将被 研究了 光谱特性将在溶液中测量， 在金属表面使用表面增强拉曼散射（Sers） 技术. Sers和表面增强共振拉曼散射 （SERRS）光谱将用于探测蛋白质的拓扑结构， 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 系统，包括天然的Langmuir-Blodgett转移单层， 和突变复合物，也由脂质或合成聚合物稳定 并吸收在SERS活性表面上，将是必不可少的详细 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.