Bioinorganic Enzymology of a Non-Heme Iron Hydroxylase

非血红素铁羟化酶的生物无机酶学

• 批准号: 0502391
• 负责人: Mahdi Abu-Omar
• 金额: $ 44万
• 依托单位: Purdue University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 2005
• 资助国家: 美国
• 起止时间: 2005-09-01 至 2008-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=0502391&HistoricalAwards=false
• 关键词: Bioinorganic; Enzymology; Non; Heme; Iron

Dr. Mahdi Abu-Omar, Chemistry Department, Purdue University, is supported by the Inorganic, Bioinorganic and Organometallic Chemistry Program of the Chemistry Divison to study the activity and substrate recognition in phenylalanine hydroxylase (PAH), a mononuclear non-heme iron hydroxylase.The reactions of nitric oxide with ferrous PAH will be used to spectroscopically model and probe the catalytically relevant iron(II) coordination environment of the early stages of O2 binding and activation in non-heme hydroxylases. The molecular structure of the quaternary complex of the enzyme with nitric oxide will be determined. Drop coating deposition Raman spectroscopy will be utilized to characterize molecular changes in the enzyme as well as in the substrates upon binding to the active site.The function of an important enzyme, phenylalanine hydroxylase, which synthesizes an essential amino acid, tyrosine that is further metabolized to important neurotransmitters will be studied. The work will focus on how oxygen is activated at its iron-containing active site. Postdoctoral, graduate, and undergraduate students will be educated in an interdisciplinary project that spans molecular biology, protein biochemistry, chemical kinetics, and spectroscopy.

普渡大学化学系的 Mahdi Abu-Omar 博士在化学系无机、生物无机和有机金属化学项目的支持下，研究苯丙氨酸羟化酶 (PAH)（一种单核非血红素铁羟化酶）的活性和底物识别。一氧化氮与亚铁 PAH 的反应将用于光谱模型 并探讨非血红素羟化酶中 O2 结合和激活早期阶段的催化相关铁 (II) 配位环境。将测定酶与一氧化氮的四元复合物的分子结构。滴涂沉积拉曼光谱将用于表征酶以及底物与活性位点结合后的分子变化。将研究重要酶苯丙氨酸羟化酶的功能，苯丙氨酸羟化酶合成必需氨基酸酪氨酸，酪氨酸进一步代谢为重要的神经递质。这项工作将集中于氧如何在其含铁活性位点被激活。博士后、研究生和本科生将接受跨学科项目的教育，涵盖分子生物学、蛋白质生物化学、化学动力学和光谱学。