EFFECT OF PROTEIN MUTATION ON ACTIVE SITE STRUCTURE IN CYTOCHROME C

蛋白质突变对细胞色素C活性位点结构的影响

• 批准号: 8362250
• 负责人: SHAMITS SARANGI
• 金额: $ 0.19万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362250
• 关键词: Active Sites; Cytochrome c Group; Data; Electron Spin Resonance Spectroscopy; Electron Transport; Environment; Enzymes; Funding; Grant; Histidine; Iron; Ligands; Light; Link; Measures; Methionine; Mutation; National Center for Research Resources; Nitrosomonas; Oxidation-Reduction; Play; Principal Investigator; Proteins; Pseudomonas aeruginosa; Radiation; Reaction; Research; Research Infrastructure; Resources; Role; Source; Structure; United States National Institutes of Health; cost; cytochrome c; meetings; research study; structural biology

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. Fe K-edge XAS data will be measured on the electron transfer protein cytochrome c (cytc). The c-type cytochromes that have histidine-methionine (His-Met) iron coordination play important roles in electron-transfer reactions and in enzymes. The axial methionine ligand plays a major role in stabilizing the protein and maintaining a low redox potential. Protein mutations of Pseudomonas aeruginosa (Pa) and Nitrosomonas europeae (Ne) cytc show differences in rhombicity (using EPR spectroscopy) in their active site, which have been linked to perturbations in the Fe-S(Met) bond. Fe K-edge EXAFS data (BL9-3) will shed light on specific geometric structure changes at the electron-transfer active site with changes in the protein environment. The experiments will be extended to S K-edge XAS (BL4-3) to obtain quantitative information on the Fe-S covalency.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 Fe K 边缘 XAS 数据将在电子转移蛋白细胞色素 c (cytc) 上测量。具有组氨酸-蛋氨酸 (His-Met) 铁配位的 c 型细胞色素在电子转移反应和酶中发挥重要作用。轴向蛋氨酸配体在稳定蛋白质和维持低氧化还原电位方面发挥着重要作用。铜绿假单胞菌 (Pa) 和欧洲亚硝化单胞菌 (Ne) cytc 的蛋白质突变在其活性位点表现出菱形差异（使用 EPR 光谱），这与 Fe-S(Met) 键的扰动有关。 Fe K 边缘 EXAFS 数据 (BL9-3) 将揭示电子转移活性位点的特定几何结构随着蛋白质环境的变化而变化。该实验将扩展到 S K-edge XAS (BL4-3)，以获得 Fe-S 共价键的定量信息。