ORIENTATION OF FMO PROTEIN IN PHOTOSYNTHETIC BACTERIA

光合细菌中 FMO 蛋白的定位

• 批准号: 8361378
• 负责人: MICHAEL L GROSS
• 金额: $ 1.26万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-01-01 至 2011-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361378
• 关键词: Architecture; Cell membrane; Chlorobi; Complex; Energy Transfer; Ensure; Funding; Grant; Individual; Mass Spectrum Analysis; Membrane; National Center for Research Resources; Organism; Pathway interactions; Peripheral; Pigments; Principal Investigator; Protein Binding; Proteins; Reaction; Research; Research Infrastructure; Resources; Source; Structure; United States National Institutes of Health; biomedical resource; cost; 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 在光合生物体中观察到的高激发能量传递效率取决于单个蛋白质复合物中的最佳色素 - 蛋白质结合几何形状以及光系统的整体结构。在绿色硫细菌中，膜连接的Fenna-Matthews-Olson（FMO）天线蛋白充当“线”，可将大型外周氯质体天线复合物与反应中心（RC）连接起来，该复合中心（RC）嵌入了细胞质膜中。氯化体收集的能量通过FMO漏斗到RC。 已经扩大了巨大的努力，以了解单个孤立粒子的结构和功能之间的关系。 FMO蛋白如何与体内膜和氯化体相互作用以维持特定结构以确保高效的能量传递途径的问题。