XAS AS A NOVEL PROBE OF ELECTRONIC STRUCTURE AND REACTIVITY FOR PROTEIN-BASED SU

XAS 作为蛋白质 SU 电子结构和反应性的新型探针

• 批准号: 7722039
• 负责人: PIERRE KENNEPOHL
• 金额: $ 0.23万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7722039
• 关键词: Anions; Biological; Biological Process; Buffers; Catalysis; Computer Retrieval of Information on Scientific Projects Database; Disease Pathway; Disulfides; Electron Spin Resonance Spectroscopy; Electron Transport; Electronics; Electrons; Environment; Funding; Goals; Grant; Hydrogen Bonding; Institution; Methionine; Neurodegenerative Disorders; Ocular orbit; Oxidation-Reduction; Peptides; Post-Translational Protein Processing; Proteins; Range; Research; Research Personnel; Resources; Roentgen Rays; Senile Plaques; Signal Transduction; Source; Spectrum Analysis; Structure; Sulfur; System; United States National Institutes of Health; absorption; base; novel; tool

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. The basic reactivity of sulfur-centered radicals is being studied in a variety of peptide/protein systems using Sulfur K-edge X-ray Absorption Spectroscopy (S K-edge XAS) as a novel probe of the electronic structure of these biologically-important peptidic radicals. Cysteinyl radicals ([CysS?]), their sulfoxyl derivatives ([CysSOn]?) disulfide anion radicals ([CysS?SCys]1-) have been observed or postulated as intermediates in several biological functions including enzymatic catalysis, long-range electron transfer, peptide post-translational modification, cellular redox buffering, and even cellular redox signaling. Methionine radicals ([MetS?]) are believed to be involved in neurodegenerative diseases pathways such as the formation of amyloid-? plaques. Electron paramagnetic resonance is the primary tool used for characterization of radical species but this approach is complicated by spin orbit broadening in sulfur species. The S 3p?1s pre-edge transition that results from radical character on a sulfur atom is being used to directly probe the electronic structure of these radicals and to investigate the effect of factors such as hydrogen bonding and electron delocalization on the reactivity of these radicals in various protein environments. An important goal of this effort is to develop S K-edge XAS as a powerful and general probe of sulfur radical species to investigate a wide range of biological systems.

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。 正在使用硫 K 边缘 X 射线吸收光谱 (SK-edge XAS) 作为这些具有生物学重要性的肽自由基的电子结构的新型探针，在各种肽/蛋白质系统中研究以硫为中心的自由基的基本反应性。半胱氨酰自由基 ([CysS?])、其磺酰基衍生物 ([CysSOn]?) 二硫阴离子自由基 ([CysS?SCys]1-) 已被观察或假设为多种生物功能的中间体，包括酶催化、长程电子转移、肽翻译后修饰、细胞氧化还原缓冲，甚至细胞氧化还原信号传导。蛋氨酸自由基（[MetS？]）被认为参与神经退行性疾病途径，例如淀粉样蛋白-？牌匾。电子顺磁共振是用于表征自由基物质的主要工具，但这种方法由于硫物质的自旋轨道展宽而变得复杂。由硫原子上的自由基特征产生的S 3p?1s 前边跃迁被用来直接探测这些自由基的电子结构，并研究氢键和电子离域等因素对这些自由基在各种蛋白质环境中的反应性的影响。这项工作的一个重要目标是开发 SK-edge XAS 作为硫自由基物种的强大且通用的探针，以研究广泛的生物系统。