With this award from the Major Research Instrumentation Program (MRI) and support from the Chemistry Research Instrumentation Program (CRIF), Professor R. David Britt from the Department of Chemistry at the University of California-Davis (UCD) and colleague Neville Luhmann from the Department of Electrical and Computer Engineering at UCD as well as various senior personnel from California, Oregon, Massachusetts and Florida will develop a pulsed EPR spectrometer that will work at a high frequency (260 GHz), with low power (50 W), and bandwidth (20 GHz) capable of carrying out electron nuclear double resonance (ENDOR) methods and double electron-electron resonance (DEER). The heart of the spectrometer design is a compact 260 GHz Sheet Beam Traveling Wave Tube (SBTWT) amplifier operating at a voltage of 20 kV with a 1% pulse duty cycle. The design is scaled from that of a 220 GHz SBTWT developed under the DARPA HiFIVE program. An industrial partner (Bridge 12) is also going to be involved. In general, an EPR spectrometer yields detailed information on the geometric and electronic structure of molecular and solid state materials. It may also be used to obtain information about the lifetimes of free radicals, short-lived, highly reactive species involved in valuable chemical transformations as well as the initiation of pathological tumor growth. These studies will impact a number of areas, from the synthesis of inorganic and organic molecules to the development of new solid state materials to compounds of magnetic and biological interest. Importantly, participation of students will allow preparation of the new generation of instrumentalists.
This award will produce an instrument capable of carrying out a series of high impact research in various interdisciplinary fields while involving multiple departments across the United States. The award is aimed at enhancing research and education at all levels, especially in areas such as (a) using Gd(III)-DPTA labeling; (b) studying mechanisms of activation in proteins of GPCR signal transduction; (c) studying how metals bind to the antimicrobial Calprotectin S100-family protein; (d) using ENDOR to probe a high affinity Mn(II) binding site in the catalytically active Mn-substituted form of the hammerhead ribosome; (e) studying oxidation of Mn(II) in manganese dioxide biomineralization by the bacterial multicopper oxidase MnxG; (f) studying the circadian clock of cyanobacteria; (g) analyzing the effects of metal ion binding in activity of DNA polymerase; (h) studying how metal ion binding affects protein folding and misfolding in a variety of proteins with Cu(II) and Zn(II) binding domains; (i) studying water oxidation and hydrogen reduction catalysts to be employed in solar fuel systems.
