PULSED X BAND EPR SPECTROMETER FOR BIOMEDICAL RESEARCH

X波段脉冲能力将被添加到伊利诺伊大学厄巴纳/香槟分校的各种电子磁共振仪器中。这将为这个校园里庞大而强大的生物医学研究社区，包括九个指定的主要用户群体，提供一个亟需的结构生物学最先进的工具。该仪器将放置在伊利诺伊州EPR研究中心(IERC)化学学院的空间内，并将由IERC操作和管理。此次升级选择的仪器是Bruker X波段ELEXYS FT-EPR光谱仪系统，该系统将整合现有的CW Bruker 300系列EPR光谱仪。ELEXYS E580 FT-EPR光谱仪是新一代最先进的仪器，能够在X波段进行几乎所有类型的现代连续和脉冲EPR实验。谢尔盖·迪卡诺夫博士是先进的脉冲电子磁共振及其在涉及金属蛋白和自由基的生物医学问题上的应用方面的世界领先专家之一，他对E580光谱仪系统有着丰富的直接经验，他将直接负责操作和维护，并将帮助所有用户使用该仪器有效地设计和解释他们的研究项目。九个主要的用户项目集中在以下主题上：用于诊断MRI的造影剂(项目1，R.B.Clarkson教授，和#2，P.Petillo教授)；蛋白质折叠中间体(项目#3，教授。研究领域包括：Bc1复合体中的电子转移(A.R.克罗夫茨教授和S.Dikanov博士)；泛喹酚氧化酶(R.B.Gennis教授)，金属酶蛋白质设计与工程(Y.Lu教授)；维生素B12依赖酶、细胞色素c氧化酶和前列腺素合成酶的作用机制(W.van der Donk教授)；蛋白质微球和血红素蛋白质类似物(K.S.Suslick教授)；以及高温稳定的古生菌Rieske型蛋白质(S.Dikanov博士)。预计本机构内外还将有许多其他重要用户。作为例子，描述了四个较小的用户项目：钒的胰岛素模因(C.Orvig教授，不列颠哥伦比亚省)；细胞色素c P-450系统中的结构-功能关系(S.斯利格教授，美国伊利诺伊州)；不可还原和神经元一氧化氮合酶中非血红素复合体的结构(D.Stuehr博士，克利夫兰诊所)；单体、还原二聚体和蛋白质结合形式的二亚硝基铁络合物的配位几何(A.Vanin，Russ。阿卡德。科学)。

X-band pulsed capability will be added to the extensive assortment of electron magnetic resonance instrumentation at the University of Illinois at Urbana/Champaign. This will provide the large and strong biomedical research community on this campus, including the nine named major- user groups, with a much needed state-of-the art tool for structural biology. The instrument will be sited in Illinois EPR Research Center (IERC) space within the School of Chemical Sciences and will be operated and managed by the IERC. The instrument chosen for this upgrade is the Bruker X-band ELEXYS FT-EPR Spectrometer System, which will incorporate the existing CW Bruker 300-series EPR spectrometer. The ELEXYS E580 FT-EPR spectrometer is a new- generation state-of-the-art instrument that is capable of performing almost all types of modern CW and pulsed EPR experiments at X-band. Dr. Sergei Dikanov, who is one of the world's leading experts in advanced pulsed electron magnetic resonance and its applications to biomedical problems involving metalloproteins and radicals and who has extensive direct experience with the E580 spectrometer system, will be in direct charge of operation and maintenance and will assist all users in effective design and interpretation of their research projects using this instrumentation. The nine major user projects focus on the following topics: contrast agents for diagnostic MRI (projects #1, Prof. R.B. Clarkson, and #2, Prof. P. Petillo); protein folding intermediates (project #3, Profs. A.I. Smirnov and R.L. Belford); electron transfer in bc1 complex (Prof. A.R. Crofts and Dr. S. Dikanov); ubiquinol oxidases (Prof R.B. Gennis), metalloenzymes protein design and engineering (Prof Y. Lu); mechanisms in vitamin B12-dependent enzymes, cytochrome c oxidase, and prostaglandin synthase (Prof. W. van der Donk); protein microspheres and heme protein analogs (Prof. K.S. Suslick); and hyperthermostable archaeal Rieske-type proteins (Dr. S. Dikanov). Many other significant users are expected from both inside and outside this institution. As examples, four minor user projects are described: insulin memesis by vanadium (Prof. C. Orvig, U. British Columbia); structure-function relationships in cytochrome c P-450 systems (Prof S. Sligar, U. Illinois); structure of NO-heme complex in irreducible and neuronal NO synthases (Dr. D. Stuehr, Cleveland Clinic); coordination geometry of dinitrosyl iron complexes in monomeric, reduced dimeric, and protein-bound forms (A. Vanin, Russ. Acad. Sci.).