XAS ELECTRONIC AND GEOMETRIC STRUCTURE STUDIES ON CU CONTAINING METALLOPROTEINS

含铜金属蛋白的 XAS 电子结构和几何结构研究

• 批准号: 8170185
• 负责人: KEITH O HODGSON
• 金额: $ 1.46万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170185
• 关键词: Active Sites; Binding; Biogenesis; Biology; Complex; Computer Retrieval of Information on Scientific Projects Database; Copper; Electron Transport; Electronics; Funding; Grant; Heme; Hydrogen Bonding; Institution; Light; Metalloproteins; Mononuclear; Pathway interactions; Property; Proteins; Proton Pump; Research; Research Personnel; Resources; Site; Source; Spectrum Analysis; Structure; Study models; System; United States National Institutes of Health; cofactor; electronic structure; 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. We propose to extend our previous studies on copper sites in biology, using a combination of S K-, Cu L-, and Cu K-edge and EXAFS spectroscopies, to define the electronic and geometric structure of Cu-containing proteins involved in electron transfer, O2 activation, N2O reduction and cofactor biogenesis. We plan to study H-bonding mutants of blue-copper proteins to evaluate the changes in electronic structure and its effect on the ET properties of BC proteins. A Cu K-edge EXAFS study will be performed on the reduced form of CuA at different pH?s to investigate the effect of pH on the ET and proton-pumping properties of the site. We also plan to study model complexes of mononuclear, binuclear, and multinuclear Cu and Heme-Cu containing proteins that are involved in O2 binding, transport and activation to understand mechanistic pathways of O2 interaction and activation. The model study will be extended and correlated to relevant protein systems to shed light on structure/function correlation of O2 binding and activation by the unique protein active sites.

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。 我们建议扩展我们以前的研究在生物学中的铜网站，使用S K-，铜L-，铜K-边和EXAFS光谱的组合，定义的电子和几何结构的含铜蛋白质参与电子转移，O2激活，N2 O还原和辅因子生物合成。我们计划研究蓝铜蛋白的氢键突变体，以评估电子结构的变化及其对BC蛋白ET性质的影响。一个铜K边EXAFS研究将在不同的pH值下的还原形式的CuA？研究pH值对该地点ET和质子泵送特性的影响。我们还计划研究模型复合物的单核，双核和多核铜和血红素铜蛋白参与O2的结合，运输和激活，以了解O2的相互作用和激活的机制途径。该模型研究将被扩展并与相关蛋白质系统相关联，以阐明O2结合和激活的独特蛋白质活性位点的结构/功能相关性。