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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 我们建议扩展我们之前对生物学中铜位点的研究，结合使用SK-、Cu L-和Cu K-边缘以及EXAFS光谱，来定义参与电子转移的含铜蛋白质的电子和几何结构、O2 活化、N2O 还原和辅因子生物发生。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特性的影响。 Cu K 边缘 EXAFS 研究将在不同 pH 值下对 CuA 的还原形式进行，以研究 pH 值对该位点的 ET 和质子泵特性的影响。我们还计划研究参与 O2 结合、运输和激活的单核、双核和多核 Cu 和血红素-Cu 蛋白的模型复合物，以了解 O2 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，以揭示 O2 结合和独特蛋白质活性位点激活的结构/功能相关性。