S. Colette Daubner, Ph.D., loves opening young people’s minds to the incredible processes by which biology gives rise to complex organisms that grow, reproduce and survive in a universe governed by chemistry and physics.
Her fascination with the biological sciences broadened as she pursued a B.S. in Zoology from the University of Wisconsin-Milwaukee, where her favorite courses were Organic Chemistry, Ichthyology, and Tolstoy and Dostoevsky. She received her Ph.D. in Biological Chemistry from the University of Michigan purifying and studying the enzyme methylenetetrahydrofolate reductase (MTHFR), an important enzyme in thymidine synthesis. MTHFR was later found to play a role in cardiovascular disease, strokes and neural tube defects. Her postdoctoral work at the Pennsylvania State University centered on the enzymes of purine de novo biosynthesis, which also utilize derivatives of folate, and are also important in fast-growing cells such as cancers and embryonic tissues.
As a research scientist in the Department of Biochemistry and Biophysics at Texas A&M in College Station, Daubner worked on the enzymes tyrosine hydroxylase (TyrH), phenylalanine hydroxylase and tryptophan hydroxylase. This family of rate-limiting enzymes uses the cofactor biopterin and bound iron to hydroxylate aromatic amino acids. Her work brought together enzymological techniques, protein modification, cloning and mutagenesis of the proteins, fluorimetry and other biophysical techniques.
Daubner left Texas A&M to join the Department of Biological Sciences at St. Mary’s. While she enjoys conducting research of her own, she finds more pleasure in introducing interested students into the world of bench experimentation.
Lou, Haiyan, Montoya, Susana E., Alerte, Tshianda N. M., Wang, Jian, Peng ,Xiangmin, Hong, Chang-Sook, Mader, Samantha A., Pedersen, Courtney J., Marcus, Brian S., McCormack, Alison L., Di Monte, Donato A., Daubner, S. Colette, and Perez, Ruth G., (2010) α-Synuclein-Mediated Regulation of Tyrosine Hydroxylase and Protein Phosphatase 2A in vitro and in vivo: Role of α-Synuclein Serine 129 Phosphorylation, J. Biol Chem 285,17648-61.
Tormos, José R., Taylor, Alex, Daubner, S. Colette, Hart, P. John, and Fitzpatrick, Paul F. (2010), Identification of a Hypothetical Protein from Podospora anserina as a Nitroalkane Oxidase Biochemistry 49, 5035-41.
Li J, Ilangovan U, Daubner, S. Colette, Hinck Andrew P, Fitzpatrick Paul F. (2011) Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase. Arch. Biochem. Biophys. 505, 250-5
Daubner, S. Colette, Le, Tiffany, and Wang, Shanzhi (2010), The R Domain of Tyrosine Hydroxylase and Regulation of Dopamine Synthesis. Arch. Biochem. Biophys. 508, 1-12.
Wang, Shanzhi, Lasagna, Mauricio, Daubner, S. Colette, Reinhart, Gregory, and Fitzpatrick, Paul F (2011) Effect of Phosphorylation of Tyrosine Hydroxylase on the Dynamics of the Regulatory Domain, Biochemistry 50, 2364-70
Daubner, S Colette Avila, Audrey M., Bailey, Johnathan, Barrera, Dimitrios, Bermudez, Jacklyn Y., Giles, David, Olivas, Crystal A., Shaheen, Noel, Thompson, Janie, Vasquez, Jessica, Oxley, Susan, and, Fitzpatrick, Paul F., (2013) Mutagenesis of a Specificity-Determining Residue in Tyrosine Hydroxylase Establishes that the Enzyme is a Robust Phenylalanine Hydroxylase but a Fragile Tyrosine Hydroxylase, Biochemistry, 52, 1446-55.