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Office: On Leave Away
Phone: 641-269-4398
Email: trimmere@grinnell.edu
B.A., 1988, Carleton College.
Ph.D. in biological chemistry. 1997, Massachusetts Institute of Technology.
NIH Postdoctoral fellow 1997-2000, University of Michigan.
Professor Trimmer is interested in the structure and mechanism of enzymes. Her
research has focused on enzymes that perform oxidation/reduction reactions using
the coenzyme flavin. She is investigating how the protein environment influences
the chemical reactivity of the flavin.
[Full description PDF]
- BCM 262 Introduction to Biological Chemistry
- CHM 129 General Chemistry
- CHM 221 Organic Chemistry I
- CHM 222 Organic Chemistry II
- CHM 330 Enzyme Mechanisms
- Trimmer, E.E., Ballou, D.P., Galloway, L.J., Scannell, S.A., Brinker, D.R, and Casas, K.R. 2005. Aspartate 120 of Escherichia coli Methylenetetrahydrofolate Reductase: Evidence for Major Roles in Folate Binding and in Catalysis, Minor Role in Flavin Reactivity. Biochemistry, 44, 6809-6822.
- Ballou, D.P., Yamada, K., Pejchal, R., Ludwig, M.L., Matthews, R.G., Trimmer, E.E. 2002. Studies of the Mechanisms of Bacterial and Mammalian Methylenetetrahydrofolate Reductases, in "Flavins and Flavoproteins 2002," (R.N. Perham ed.), pp. 13-22.
- Trimmer, E.E., Ballou, D.P., Matthews, R.G. 2001. Methylenetetra-hydrofolate Reductase from Escherichia coli: Elucidation of the Kinetic Mechanism by Steady-State and Rapid-Reaction Studies. Biochemistry, 40, 6205-6215.
- Trimmer, E.E., Ballou, D.P., Ludwig, M.L., Matthews, R.G. 2001. Folate Activation and Catalysis Methylenetetrahydrofolate Reductase from Escherichia coli: Roles for Aspartate 120 and Glutamate 28. Biochemistry, 40, 6216-6226.
- Sheppard, C.A., Trimmer, E.E., Matthews, R.G. 1998. Purification and Properties of NADH-dependent 5,10-Methylenetetrahydrofolate Reductase (MetF) from Escherichia coli. J. Bacteriology, 181, 718-725.
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