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- B.A. (Chemistry), Harvard University, 1962
- Ph.D. (Inorganic chemistry), Massachusetts Institute of Technology, 1972
- John Evans Professor; Department of Chemistry and Biochemistry, University of Denver, 1997- present
- Professor; Department of Chemistry, University of Denver, 1980 - 1997
- Vice Provost for Research; University of Denver, 1988-89
- Dean of Natural Sciences; University of Denver, 1984-88
- Associate Professor; Department of Chemistry, University of Denver, 1976-80
- Assistant Professor; Department of Chemistry, University of Denver, 1972-76
- Postdoctoral Research Associate; Department of Chemistry, Massachusetts Institute of Technology
- University Lecturer, University of Denver, 1988
- Special Award of the International EPR/ESR Society, 1996
- University of Denver Evans Professorship, 1997
- American Chemical Society, Colorado Section Award, 2001
- Bruker Prize, awarded by the Royal Society of Chemistry, EPR Discussion Group, 2002
How to Contact Me
office: Seeley Mudd Rm. 159
mail: Department of Chemistry and Biochemistry
University of Denver
2101 E. Wesley Ave.
Denver, CO 80208
Materials for classes that I am teaching are on the Blackboard sites for those courses
Electron paramagnetic resonance (EPR) (also known as electron spin resonance (ESR)) studies of molecules with unpaired electrons - primarily organic radicals and transition metal ions. We are interested in a variety of applications of this technique.
EPR imaging examines the spatial distribution of unpaired electrons in a sample. We are developing CW, pulsed, and rapid scan imaging methodologies for in vivo applications.
Electron spin relaxation times are measured by pulsed EPR techniques. The relaxation times provide insight into molecular dynamics. Measurements at multiple resonance frequencies permit assignment of mechanisms.
Pulsed EPR techniques can measure weak interactions between transition metal ions and nuclear spins in proximity to the metal. This technique is a powerful method to examine the metal binding sites in metalloenzymes. We have applied it to the iron binding site in transferrin, and to other metalloenzymes brought to us by collaborators.
Pulsed and CW EPR techniques provide a range of techniques for measuring interspin distance and we have applied these to spin-labeled metmyoglobin, spin-labeled carbonic anhydrase, and other biomolecules containing two unpaired electrons.
This portfolio last updated: Sep 23, 2012 11:21:01 AM