X-RAY ABSORPTION STUDIES OF MUTANTS OF COPPER/ZINC SUPEROXIDE DISMUTASE

铜/锌超氧化物歧化酶突变体的X射线吸收研究

• 批准号: 7598014
• 负责人: SERENA D DE BEER GEORGE
• 金额: $ 0.18万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7598014
• 关键词: Amyotrophic Lateral Sclerosis; Computer Retrieval of Information on Scientific Projects Database; Electronics; Enzymes; Exhibits; Funding; Grant; Institution; Research; Research Personnel; Resources; Roentgen Rays; Series; Site; Source; Spectrum Analysis; Structure; Superoxide Dismutase; Toxic effect; United States National Institutes of Health; absorption; copper zinc superoxide dismutase; insight; mutant

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. X-ray absorption spectroscopy (XAS) will be used to investigate a series of copper-zinc superoxide dismutase (CuZnSOD) mutants. These mutants all exhibit a decrease in SOD activity and also show perturbations in the EPR and UV-vis spectra of the oxidized enzymes. Cu(II) K-edge XAS will allow for further characterization of the electronic and geometric structure of the oxidized enzyme. Cu(I) K-edge XAS will allow for characterization of the reduced enzyme, which will aid in understanding any alteration in the mechanism in these mutants. Zn K-edge XAS will be used to determine if any changes have occurred at the structural Zn site. These results will be compared to XAS studies on the WT enzyme and may provide important insight into mutant SOD1 enzyme toxicity in amyotrophic lateral sclerosis (ALS).

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 X射线吸收光谱(XAS)将用于研究铜锌超氧化物歧化酶(CuZnSOD)的一系列突变体。这些突变体都表现出超氧化物歧化酶活性的下降，并在氧化酶的EPR和UV-Vis光谱中表现出扰动。铜(II)K-EDGE XAS可以进一步表征氧化酶的电子结构和几何结构。铜(I)K-EDGE XAS将允许表征还原的酶，这将有助于理解这些突变体机制中的任何变化。将使用锌K边XAS来确定结构锌位置是否发生了任何变化。这些结果将与XAS对WT酶的研究进行比较，并可能为肌萎缩侧索硬化症(ALS)中突变的SOD1酶的毒性提供重要的见解。