Sharon J. Nieter Burgmayer
Professor
Inorganic Chemistry
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Sharon J. Nieter Burgmayer Inorganic Chemistry |
Born, 1956. B.S., Heidelberg College, 1979. Ph.D., University of North Carolina, 1984. Postdoctoral research, Exxon Corporate Research, 1984-1986. Phone: (610)526-5106; e-mail: sburgmay@brynmawr.edu; for more information on research, see: Burgmayer Research Group Page
Within the area of bioinorganic chemistry, the attention of my research group is focused on those metalloenzymes that require a pterin cofactor. The metals represented in this group are iron, copper, molybdenum, and tungsten. The pterin portion is a nitrogen heterocycle related to the familiar nucleic acid guanine. These enzymes are widely distributed throughout Nature where they performorganic redox reactions, primarily hydroxylations, that are critical to the health of the organism. Both the metal and the pterin have a rich and complicated redox reactivity in the absence of the protein coat and this fact underlies many of our projects concerned with questions of how metals and pterins behave in redox reactions, both individually and with each other. The specific tether that connects the molybdenumor tungsten atomto the pterin cofactor is a dithiolene; an illustration of the molybdenumcofactor of the bacterial enzyme DMSO reductase is shown below opposite one of our target model complexes. A second set of projects involves the development of syntheses for producing such target model complexes having pterin-dithiolene ligands coordinated to molybdenum. These projects involve both inorganic and organic syntheses, many of which are performed under inert atmosphere environments. The synthetic products and their chemical reactivity are studied by spectroscopic analysis, electrochemical characterization, kinetic studies, structure determination by x-ray crystallography, and molecular modeling. Routine spectroscopic techniques such as FT-NMR, FT-IR, UV-vis, and fluorescence are conducted in the Bryn Mawr chemistry department. Certain projects require other techniques, such as EPR or XPS, that are accomplished through collaborations with researchers at other institutions.
"A Model Reaction for Molybdenum(VI) Reduction by Molybdopterin," S. J. N. Burgmayer, A. Baruch, K. Kerr, and K. Yoon, Journal of the American Chemical Society 1989, 111, 4982.
"Resonance Raman Signatures of Oxomolybdenum Thiolate and Dithiolene Models of Molybdenum Proteins," P. Subramanian, S. Burgmayer, S. Richards, V. Szalai, and T. G. Spiro, Inorganic Chemistry 1990, 29, 3849.
"Preparations and Properties of Transion-Metal Pterin Complexes. Models for the Metal Site in Phenylalanine Hydroxylase," J. Perkinson, S. Brodie, K. Yoon, K. Mosny, P. J. Carroll, T. V. Morgan, and S. J. N. Burgmayer, Inorganic Chemistry 1991, 30, 719.
"Oxidation of Molybdenum Dithiolene Complexes Yields Thiophene Analogs of Urothione and Molybdopterin Form B," C. L. Soricelli, V. A. Szalai, and S. J. N. Burgmayer, Journal of the American Chemical Society 1991, 113, 9877.
"Molybdenum Complexes of Reduced Pterins," S. J. Burgmayer, K. Everett, and L. Bostick In Molybdenum Enzymes, Cofactors and Model Systems, Stiefel, E. I., Coucouvanis, D., Newton, W., Eds.; ACS Symposium Series 535; American Chemical Society: Washington, D.C., 1993; p 114.
"Tetrahydropterin Reactions of Dioxo-Molybdenum(6+) Complexes. Does Redox Occur?" S. J. N. Burgmayer, M. R. Arkin, L. Bostick, S. Dempster, K. Everett, H. Layton, K. Paul, and C. Rogge, Journal of the American Chemical Society 1995, 117, 5812.
"Electron Transfer in Transition Metal Pteridine Systems," S. J. N. Burgmayer In Bioinorganic Chemistry of the Less Common Metals, Clarke, M. J., Ed.; Springer-Verlag: Heidelberg, in press.
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