Jennifer L. DuBois
Office: room 218
lab: room 220
Chemistry and Biochemistry Building
P.O. Box 173400
Bozeman, MT 59717
University of California Berkeley, NIH postdoctoral fellow
Stanford University, Ph.D. Chemistry
Cornell University, B.A. Biochemistry
Our research is inspired by the spectacular diversity of microbes and gene products that have come to light in the post-genomic age. Microbial life has adapted to every imaginable environmental niche – from the human gut to the hot spring – in part by evolving an array of protein-based catalysts. Our longstanding expertise is with biocatalytic processes exploiting atmospheric oxygen and its partners – iron, heme, copper, organic cofactors, or sometimes just a protein environment alone. These carry out reactions that may be essential for bacterial pathogenicity, or which can solve economically important problems in a chemically green way. We likewise are focusing on microbial reactions that couple a redox step to the release or fixation of atmospheric carbon dioxide gas. Studying these catalytic processes has led us to fundamental discoveries about how microbes interact with their environments to acquire and repackage the iron and heme that drive their redox “engines”.
Chemistry 102 CS: Chemistry and Society
Chemistry 123: Introductory Organic and Biological Chemistry
Chemistry 350: Astrobiology
Celis, A. I.; Gauss, G.H.; Streit, B. R.; Shisler, K.; Moraski, G. C.; Rodgers, K. R.; Lukat-Rodgers, G. S.; Peters, J. W.; DuBois, J. L. (2017) Structure-based mechanism for decarboxylation reactions mediated by amino acids and heme propionates in coproheme decarboxylase (HemQ). J. Am. Chem. Soc., 139, 1900-1911.
Prussia, G. A.; Gauss, G. H.; Mus, F.; Conner, L.; DuBois, J. L.; Peters, J. W. (2016) Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity. FEBS Lett., 590, 2991-2996.
Streit, B.R., Kant, R., Tokmina-Lukaszewska, M., Celis, A.I., Machovina, M.M., Skaar, E.P., Bothner, B., DuBois, J.L. (2016) “Time-resolved Studies of IsdG Protein Identify Molecular Signposts along the Non-canonical Heme Oxygenase Pathway.” J. Biol. Chem.291: 862-871.
Machovina, M. M.; Usselman, R. J.; DuBois, J. L. (2016) Monooxygenase substrates mimic flavin to catalyze cofactorless oxygenations. J. Biol. Chem., 291, 17816-28.
DuBois, J. L., Ojha, S. “Production of Dioxygen in the Dark: Dismutases of Oxyanions,” (2015) Metal Ions in Life Sciences, Wiley and Sons, volume 15, Guest Editors: P.M. H. Kroneck and M.E. Sosa-Torres; Series editors: A.Sigel, H. Sigel, and R. K. O. Sigel, pp. 45-87.