Colleen Byron

 

Colleen Byron

Education

  • B.A., chemistry, College of St. Benedict, St. Joseph, Minn.
  • Ph.D., analytical chemistry, University of Minnesota, Minneapolis, Minn.

Professional Activities

  • American Chemical Society
  • Project Kaleidoscope: Faculty for the 21st Century
  • Midwest Association of Chemistry
  • Teachers at Liberal Arts Colleges

Current Courses Taught

  • Quantitative Chemical Analysis
  • Chemical Instrumentation, Biochemistry
  • Chemistry in Context: Global Chemistry, First-Year Studies.
  • Senior Seminar

 

Awards and Honors

  • James R. Underkofler Excellence in Teaching Award, April, 2011
  • Ripon College Senior Awards, 1995, 2004
  • May Bumby Severy Teaching Awards, 1995, 2002
  • Merck/AAAS Undergraduate Science Program Grant ($60,000), 2002
  • National Science Foundation CAREER Program Grant ($128,000), 1995

 

Recent Publications and Presentations

  • Secondary Coenzyme Q10 Deficiency and Oxidative Stress in Cultured Fibroblasts from Patients with Riboflavin Responsive Multiple Acyl- CoA Dehydrogenation Deficiency. N. Cornelius, C. Byron, I.Hargreaves, P. F. Guerra, A. K. Furdek*, J. Land, W. W. Radford*, F. Frerman, T. J. Corydon, N. Gregersen, and R. K. J. Olsen (2013) Human Molecular Genetics, accepted May 2013, in press.
  • 245th American Chemical Society National Meeting, April 7-13, 2013, New Orleans, LA. “Effects of 4-Hydroxy-2-Nonenal on Electron Transfer Flavoprotein” C. M. Byron, S. B. Sondalle*, H. M. Nennig*, J. A. Rindt *, and F. E. Frerman.
  • The Effect of 4-Hydroxy-2-Nonenal on the Activities of Electron Transfer Flavoprotein and Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase Sondalle, S. B.*, Byron, C. M., Nennig, H. M.*, Rindt, J. A.*, and Frerman, F. E. (2013) in Flavins and Flavoproteins 2011 (Miller, S., Hille, R., and Palfey, B., Eds.) pp 417- 422, Lulu, Raleigh, NC.
  • Use of Brominated Pseudosubstrates for Fluorescence Quenching Studies of Wild Type and Riboflavin Responsive Clinical Mutants of Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase (ETF-QO). Byron, C.M., Furdek, A.K.*, Radford, W.W.* and Frerman, F.E. (2008) in Flavins and Flavoproteins 2008 (Frago, S., Gómez-Moreno, C. and Medina, M., eds.) pp 131-134,Prensas Universitarias de Zaragoza, Zaragoza, Spain.
  • 16th International Symposium on Flavins and Flavoproteins, June 8-13, 2008, Palacio de Congresos, Jaca, SPAIN. “Use of Brominated Pseudosubstrates for Fluorescence Quenching Studies of Wild Type and Riboflavin Responsive Clinical Mutants of Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase (ETF-QO)” C.M. Byron, A.K. Furdek*, W.W. Radford* and F.E. Frerman.
  • 233rd National American Chemical Society Meeting, March 25-29, 2007, Chicago, Ill. “Synthesis and Purification of Brominated Ubiquinone Pseudosubstrates for Fluorescence Studies of Electron-Transfer Flavoprotein: Ubiquinone Oxidoreductase (ETF:QO).” A.K. Furdek*, W.W. Radford*, F.E. Frerman and C.M. Byron.
  • “Electrochemical Properties of Free and Substrate Analog Bound Wild Type and Mutant  Human Glutaryl-CoA Dehydrogenase.” C.M. Byron, A.T. Tratar*, P.R. Lentz*, G.S. Furdek*, J.S. Jorn* and F.E. Frerman, 2005 in Flavins and Flavoproteins (Nishino, T., Miura, R., Tanokura, M. and Fukui, K., eds.) pp 215-220, ARchiTect Inc., Tokyo.
  • American Association for the Advancement of Science (AAAS) Annual Meeting, Feb. 11-13, 2005, Washington, D.C. “Concentration of Lead in Various Specimens in the Ecosystem of Rush Lake, Winnebago County, Wisconsin.” D.J. Feld*, W.S. Brooks, C.M. Byron.
  • 15th International Symposium on Flavins and Flavoproteins, April 17-22, 2005, Shonan Village Conference Center, Hayama, Japan. “Electrochemical Properties of Free and Substrate Analog Bound Wild Type and Mutant  Human Glutaryl-CoA Dehydrogenase.” C.M. Byron, A.T. Tratar*, P.R. Lentz*, G.S. Furdek*, J.S. Jorn* and F.E. Frerman.
  • The 27th Annual Midwest Environmental Chemistry Workshop, October 15-17, 2004, Madison, Wis. “Concentration of Lead in Various Specimens in the Ecosystem of Rush Lake, Winnebago County, Wisconsin.” D.J. Feld*, W.S. Brooks and C.M. Byron.
  • American Association for the Advancement of Science (AAAS) Annual Meeting, Feb. 12-14, 2004, Seattle, Wash. “Comparison of the Electrochemical Properties of R94Q Glutaryl-Coenzyme A Dehydrogenase Strain With Wild-Type.” G.S. Furdek*, P.R. Lentz*, E.C. Ferguson*, J.E. Stockton*, F.E. Frerman and C.M. Byron.
  • The 14th annual Argonne Symposium for Undergraduates in Science, Engineering and Mathematics, Oct. 24-25, 2003, Argonne National Laboratories, Argonne, Ill. “Determination of Lead Concentration in Eggshells of Six Bird Species at Rush Lake, Winnebago County, Wisconsin.” K.C. Koldon*, W.S. Brooks and C.M. Byron.
  • American Association for the Advancement of Science (AAAS) Annual Meeting, Feb. 14-16, 2003, Denver, Colo. “Comparison of the Electron Transfer Properties of Wild Type Glutaryl Coenzyme A Dehydrogenase with Clinically Relevant Mutated Forms of the Enzyme.” J.E. Stockton*, F.E. Frerman and C.M. Byron.
  • Synthesis, Activity and Complexation Effects of Glutaryl-CoA Analogs with Glutaryl-CoA Dehydrogenase. E.C. Ferguson*, L.M. Sharpe*, S.L. McKinney*, C.L. Donley*, G.K. Sewall*, A.L. Larsen* and C.M. Byron (1999) in Flavins and Flavoproteins 1999 (S. Ghisla, P. Kroneck, P. Macheroux and H. Sund, eds.) pp. 503-506, Rudolf Weber, Berlin.
  • Synthesis of Substrate Analogs for Glutaryl-CoA Dehydrogenase: 3-Thia-Glutaryl-CoA and 4-Nitrobutyryl-CoA. P.L. Kultgen*, L. Edwards, Jr.* and C.M. Byron (1997) Microchem. J., 56, 4-9.

  • * denotes student coauthors

 

Areas of Interest

  • Thermodynamic analyses of enzymes involved in fatty acid and amino acid oxidation including the mitochondrial membrane enzyme Electron Transfer Flavoprotein:Ubiquinone Oxidoreductase (ETF:QO) and the mitochondrial matrix enzyme Glutaryl-CoA Dehydrogenase (GCD) as a way of evaluating the molecular bases of the childhood diseases Glutaric Aciduria Types II and I and of Multiple Acyl-CoA Dehydrogenase Deficiencies. More specifically, the exploration of the role of ubiquinone binding to clinically relevant mutant and wild type ETF:QO through organic synthesis and fluorescence quenching analysis and spectroelectrochemical evaluation of the redox properties of mutant and wild type GCD. The chemical alteration of ETF:QO by reactive oxygen species (ROS) also is of interest.
  • Chemical analyses of Wisconsin’s environment, including evaluation of the lead content of various components of the contaminated Rush Lake ecosystem.