Mechanistic insights into nitric oxide synthase catalytic function

该奖项是根据2009年美国复苏和再投资法案（公法111-5）资助的。 无机，生物无机和有机化学计划支持克利夫兰州立大学的Mekki Bayachou博士的努力，探索一氧化氮合酶（NOS）酶从氨基酸L-精氨酸（Arg）产生NO的两步反应。 这项研究解决了有关NOS中的蛋白质环境如何控制其血红素活性位点的还原电位的基本问题，并探讨了辅因子和底物的结合如何通过改变催化过程中血红素的氧化还原电位来调节NOS的活性。 由于NO自由基具有显著的生物调节功能，目前对NO生物化学的兴趣相当大。 Bayachou教授，他的学生和他的合作者已经准备好通过开发独特的快速扫描循环伏安法和光谱电化学工具集来解决NOS酶学中许多迷人的和基本的机械问题。 本研究中开发的创新工具应广泛适用于其他血红素蛋白。

This award is funded under the American Recovery and Reinvestment Act of 2009 (Public Law 111-5). The Inorganic, Bioinorganic, and Organometallic Chemistry Program supports the efforts of Dr. Mekki Bayachou of Cleveland State University to explore the two-step reaction by which Nitric Oxide Synthase (NOS) enzymes produce NO from the amino acid L-arginine (Arg). This research addresses fundamental questions about how the protein environment in NOS controls the reduction potential of its heme active site and explores how the binding of cofactors and substrates may regulate the activity of NOSs by altering the heme's redox potential during catalysis. There is considerable current interest in NO biochemistry because of the remarkable bioregulatory functions that have been identified for the NO free radical. Professor Bayachou, his students, and his collaborators are well poised to address many fascinating and fundamental mechanistic questions in NOS enzymology through the development of unique fast-scan cyclic voltammetry and spectroelectrochemical tool sets. The innovative tools developed in this study should be widely applicable to other heme proteins.