XAS STUDIES OF THE STRUCTURE AND FUNCTION OF WEAK CHEMICAL INTERACTIONS IN PSEUD

PSEUD中弱化学相互作用的结构和功能的XAS研究

• 批准号: 7598278
• 负责人: Takamitsu Kohzuma
• 金额: $ 0.1万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7598278
• 关键词: Active Sites; Biological; Chemicals; Computer Retrieval of Information on Scientific Projects Database; Copper; Electronics; Ferns; Funding; Grant; Imidazole; Institution; Ligands; Plastocyanin; Play; Proteins; Reporting; Research; Research Personnel; Resources; Role; Signal Transduction; Source; Structure; System; United States National Institutes of Health; absorption; mutant; pseudoazurin

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. Non-covalent weak interactions play important roles in biological systems. Very recently, we reported the structure and reactivity of the Met16Phe mutant of the blue copper protein pseudoazurin (PAz) to investigate the effects of the pi-pi interaction observed in the unusual structure and reactivity of fern plastocyanin. The Met16 substituted mutants of PAz, in which several alkyl and aromatic groups are introduced close to the imidazole of the His81 ligand, have been constructed and characterized in order to probe the effects of the indirect weak interaction on the structure and function of the active site. Electronic absorption spectra of Met16Tyr, Met16Trp, and Met16Phe mutants indicated the smaller ratio of A460/A598 = ~0.3 as compared to that of wild type PAz, A460/A594 = 0.46. EPR spectra of the Met16Phe, Met16Tyr and Met16Trp mutants indicated the enhancement of the axial signal contribution. In this proposal, we will investigate the detailed structural and electronic structural information at the active site of Met16X pseudoazurin mutant proteins by XAS.

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。 非共价弱相互作用在生物系统中发挥着重要作用。最近，我们报道了蓝铜蛋白伪天青蛋白（PAz）的 Met16Phe 突变体的结构和反应性，以研究在蕨类质体蓝蛋白的不寻常结构和反应性中观察到的 pi-pi 相互作用的影响。 PAz 的 Met16 取代突变体在 His81 配体的咪唑附近引入了多个烷基和芳香基团，并进行了表征，以探讨间接弱相互作用对活性位点结构和功能的影响。 Met16Tyr、Met16Trp 和 Met16Phe 突变体的电子吸收光谱表明，与野生型 PAz 相比，A460/A598 = ~0.3 的比率更小，A460/A594 = 0.46。 Met16Phe、Met16Tyr 和 Met16Trp 突变体的 EPR 谱表明轴向信号贡献的增强。在本提案中，我们将通过 XAS 研究 Met16X 伪天青蛋白突变蛋白活性位点的详细结构和电子结构信息。