ORIENTATION OF FMO PROTEIN IN PHOTOSYNTHETIC BACTERIA

光合细菌中 FMO 蛋白的定位

• 批准号: 8168739
• 负责人: MICHAEL L GROSS
• 金额: $ 1.16万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-03-10 至 2010-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8168739
• 关键词: Architecture; Cell membrane; Chlorobi; Complex; Computer Retrieval of Information on Scientific Projects Database; Energy Transfer; Ensure; Funding; Grant; Individual; Institution; Membrane; Organism; Pathway interactions; Peripheral; Pigments; Protein Binding; Proteins; Reaction; Research; Research Personnel; Resources; Source; Structure; United States National Institutes of Health; 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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 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-蛋白质结合几何形状，也依赖于光系统的整体结构。在绿色硫细菌中，膜附着的Fenna-Matthews-Olson（FMO）天线蛋白作为“导线”将大的外周叶绿体天线复合物与嵌入细胞质膜中的反应中心（RC）连接起来。由叶绿体收集的能量通过FMO汇集到RC。 人们已经做出了巨大的努力来理解单个孤立粒子的结构和功能之间的关系。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传递途径的问题尚未得到回答。