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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此，可以在其他清晰的条目中表示。列出的机构是 对于中心，这不一定是调查员的机构。 我们建议使用S K-，Cu L-和Cu K-Edge和ExAFS光谱镜的结合来扩展生物学铜位点的先前研究，以定义参与电子传递的CU蛋白的电子和几何结构，O2激活，N2O还原和辅因子生物发生。我们计划研究蓝opper蛋白的H键突变体，以评估电子结构的变化及其对BC蛋白的ET特性的影响。将对不同pH的CUA的降低形式进行CU K-EDGES研究，以研究pH对位点的ET和质子泵送特性的影响。我们还计划研究模拟单核，双核和多核Cu和Heme-Cu的复合物，其中含有O2结合，运输和激活，以了解O2相互作用和激活的机械途径。模型研究将扩展并与相关的蛋白质系统相关，以阐明独特的蛋白质活性位点O2结合和激活的结构/功能相关性。