MRI: ACQUISITION OF A PULSED ELECTRON SPIN RESONANCE SPECTROMETER TO AID BIOPHYSICAL AND CHEMICAL RESEARCH, EDUCATION AND OUTREACH

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This award is supported by the Major Research Instrumentation (MRI) and the Chemistry Research Instrumentation and Facilities (CRIF) Programs. Professor Sunil Saxena from University of Pittsburgh and colleagues are acquiring an X-/Q-band pulsed electron paramagnetic resonance (EPR) spectrometer. This instrument allows research in a variety of fields such as those that provide insight on how biologically relevant species with unpaired electrons behave. The instrument also allows researchers to conduct advanced environmental studies. In general, an EPR spectrometer yields detailed information on the geometric and electronic structure of molecular and solid state materials. It is used to obtain information about the lifetimes of unpaired electrons (free radicals) - a short-lived, highly reactive species - involved in valuable chemical transformations. A number of graduate and undergraduate students use the instrument. This spectrometer expands access to pulsed EPR instrumentation to undergraduates at a 4-year college in Pennsylvania (Westminster) College) and a predominantly African American institution (Fisk University). The spectrometer furthers the development of an EPR Center of Excellence that is regional in nature, thus having a broad impact in research infrastructure for the entire tri-state area. Current users include groups at University of Pittsburgh, Carnegie Mellon University, Ohio State University, Fisk University and Westminster College. The results of the research help modernize the high-school curriculum by rapid dissemination of research ideas to high-school teachers via workshops. The spectrometer is used in classes to expose students to modern ideas in biophysics. This EPR spectrometer enhances research and education at all levels. It allows sensitive delineation of backbone versus spin label motions in proteins and macromolecules ,and enables high resolution measurements to determine constraints on macromolecular structure and conformational dynamics. The spectrometer also allows discrimination of metal-protein interactions and enables the determination of the identity of transient and stable radicals.