ORIENTATION OF FMO PROTEIN IN PHOTOSYNTHETIC BACTERIA

光合细菌中 FMO 蛋白的定位

• 批准号: 7953975
• 负责人: Robert Eugene Blankenship
• 金额: $ 1.16万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-02-01 至 2010-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7953975
• 关键词: Architecture; Cell membrane; Chlorobi; Complex; Computer Retrieval of Information on Scientific Projects Database; Energy Transfer; Ensure; Funding; Grant; Individual; Institution; Mass Spectrum Analysis; Membrane; Organism; Pathway interactions; Peripheral; Pigments; Protein Binding; Proteins; Reaction; Research; Research Personnel; Resources; Source; Structure; United States National Institutes of Health; biomedical resource; in vivo; particle; photosynthetic bacteria; photosystem; protein complex; protein function

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The high excitation energy transfer efficiency observed in photosynthetic organisms relies on the optimal pigment-protein binding geometry in the individual protein complexes and also on the overall architecture of photosystems. In green sulfur bacteria, the membrane-attached Fenna-Matthews-Olson (FMO) antenna protein functions as a "wire" to connect the large peripheral chlorosome antenna complex with the reaction center (RC), which is embedded in the cytoplasmic membrane. Energy collected by the chlorosome is funneled through the FMO to the RC. Significant effort has been expanded to understand the relationship between structure and function of the individual isolated particles. The question of how the FMO protein interacts with the membrane and the chlorosome in vivo to maintain a specific architecture to ensure the highly efficient energy transfer pathway, however, has not been answered.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 在光合生物中观察到的高激发能量转移效率依赖于单个蛋白质复合物中的最佳色素-蛋白质结合几何结构以及光系统的整体结构。在绿硫细菌中，膜附着的 Fenna-Matthews-Olson (FMO) 天线蛋白充当“电线”，将大型外围叶绿体天线复合体与嵌入细胞质膜中的反应中心 (RC) 连接起来。叶绿体收集的能量通过 FMO 输送到 RC。 为了理解单个孤立粒子的结构和功能之间的关系，人们付出了巨大的努力。然而，FMO蛋白如何在体内与膜和叶绿体相互作用以维持特定的结构以确保高效的能量转移途径的问题尚未得到解答。