Bioinorganic Enzymology of a Non-Heme Iron Hydroxylase

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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.