Bioinorganic Enzymology of a Non-Heme Iron Hydroxylase

普渡大学化学系的Mahdi Abu-Omar博士得到化学系无机、生物无机和有机化学项目的支持，研究苯丙氨酸羟化酶（PAH）的活性和底物识别，一种单核非血红素铁羟化酶。一氧化氮与亚铁PAH的反应将用于光谱模型和探测催化相关的铁（II）在非血红素羟化酶中O2结合和活化的早期阶段的配位环境。将确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结合到活性位点后的底物中的分子变化。将研究重要酶苯丙氨酸羟化酶的功能，该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。这项工作将集中在氧是如何在其含铁的活性位点被激活。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。

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.