XAS ELECTRONIC AND GEOMETRIC STRUCTURAL STUDIES OF COPPER REDOX CENTERS

铜氧化还原中心的 XAS 电子和几何结构研究

• 批准号: 7370411
• 负责人: KEITH O HODGSON
• 金额: $ 0.19万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370411
• 关键词: XAS; ELECTRONIC; GEOMETRIC; STRUCTURAL; STUDIES

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 plastocyanin, 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 electron transfer proteins. The first part of our studies will focus on the understanding the differences between classic blue Cu sites and perturbed blue copper sites. A series of native and mutant proteins, where the axial ligand is systematically varied, will provide insight into the role of the axial ligand and other factors that control redox activity in blue copper sites. The second part of our studies will focus on the CuA center of cytochrome c oxidase and nitrous oxide reductase. We are interested in determining the nature of the ground state wave function in Cu A, defining contributions to the delocalization of the site, and gaining insight into ligand field contributions to metal-metal bond formation. This will be achieved through isotropic studies at the Cu K-, S K-, and Cu L-edge, as well as through polarized Cu K- and S K-edge studies.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。我们建议扩展我们以前的研究plastocyanin，使用S K-，铜L-，铜K-边和EXAFS光谱的组合，定义含铜的电子转移蛋白的电子和几何结构。我们的研究的第一部分将集中在理解经典蓝铜网站和扰动蓝铜网站之间的差异。一系列的天然和突变体蛋白质，其中轴向配体是系统地变化，将提供洞察的轴向配体和其他因素，控制氧化还原活性在蓝铜网站的作用。第二部分研究细胞色素c氧化酶和一氧化二氮还原酶的CuA中心。我们感兴趣的是确定在Cu A的基态波函数的性质，定义的网站的离域的贡献，并深入了解配位场的贡献，金属-金属键的形成。这将通过在Cu K-，S K-和Cu L-边缘的各向同性研究，以及通过极化Cu K-和S K-边缘的研究来实现。