An electron paramagnetic resonance spectrometer will be required for studies in a wide range of biological problems. Applications of the instrument include: (1) structural and mechanistic studies of the molybdenum centrs of xanthine oxidase ans sulfite oxidase, (2) studies of the effects of chemical modificatio of plastocyanin on the structure and function of its copper center, (3) determination of the oxidation-reduction potentials of genetically engineered forms of the flavodoxin from Desulfovibrio vulgaris, (4) a spin-label study of substrate binding to xanthine oxidase aimed at establishing the Kd for binding of xanthine to the oxidized form of the enzyme and the number of substrate binding sites present in the active site, (5) use of laser-induced excitation of carbonmonoxy cytochrome c oxidase and nitrosylhemoglobin to examine changes in the EPR signals of these centers. Together, these projects constitute a major application of elctron paramagnetic resonance spectroscopy that would greatly enhance the basic research capability of an extended group of biochemists at Ohio State University.
