EXAFS STUDIES OF NON-HEME IRON ENZYME INTERMEDIATES AND MODEL COMPOUNDS

非血红素铁酶中间体和模型化合物的 EXAFS 研究

• 批准号: 7721762
• 负责人: LAWRENCE QUE, JR
• 金额: $ 0.36万
• 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/7721762
• 关键词: Chemistry; Complex; Computer Retrieval of Information on Scientific Projects Database; Dioxygen; Enzymes; Escherichia coli; Ferritin; Funding; Grant; Heme; Heme Iron; Institution; Life; Metabolic; Methane hydroxylase; Modeling; Oxygen; Play; Reaction; Reporting; Research; Research Personnel; Resources; Role; Source; Structure; United States National Institutes of Health

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 diiron centers in non-heme enzymes activate dioxygen to carry out many different important metabolic transformations. In the reactions of these enzymes with O2 various intermediates have been observed which are critical for understanding the reaction mechanisms. XAS has played a key role in establishing the core structures of some of these intermediates. We propose to use EXAFS to study the short-lived intermediates of several non-heme diiron enzymes and compare their structures with those of the three intermediates already reported. Specifically, we will study the peroxo intermediate of the ferritin from E. coli, intermediate Q of methane monooxygenase (MMO) in the presence of substrate, and metastable (but as yet not crystallized) model complexes related to the oxygen activation chemistry of these nonheme diiron enzymes.

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。子项目及 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。 非血红素酶中的二铁中心激活双氧以进行许多不同的重要代谢转化。在这些酶与 O2 的反应中，观察到了各种中间体，这对于理解反应机制至关重要。 XAS 在建立其中一些中间体的核心结构方面发挥了关键作用。我们建议使用 EXAFS 研究几种非血红素二铁酶的短寿命中间体，并将其结构与已报道的三种中间体的结构进行比较。具体来说，我们将研究大肠杆菌铁蛋白的过氧中间体、底物存在下甲烷单加氧酶 (MMO) 的中间体 Q，以及与这些非血红素的氧活化化学相关的亚稳态（但尚未结晶）模型复合物二铁酶。