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 cofactors and protein-based catalysts. Specific research questions that our projects address include:
(1) How the microbiome contributes to human nutritional iron uptake and heme metabolism. Heme from red meat is more bioavailable than non-heme forms of iron, even though there is no known heme transporter in the gut epithelia. At the same time, a causative connection between dietary heme, the microbiome, and colon cancer has been identified, though the nature of the connection is unclear. We are using constructed communities of bacteria in liquid, biofilm, and germ-free mouse models, in conjunction with state-of-the-art bioanalytical methods, to understand how bacteria contribute to host iron metabolism; the ultimate goal is to develop probiotic solutions to important human health problems including anemia and cancer. This work is funded by the NIH.
(2) How pathogenic bacteria make heme. Heme is an essential cofactor for promoting rapid growth in widespread human pathogens like Staphylococcus aureus. It was recently shown that several pathogens, including S. aureus, Streptococci, and the causative agent of tuberculosis, all synthesize and degrade heme using unexpected pathways. We are studying key catalysts in these pathways in order to better understand their function, inhibition, and origins; the long-term goal is to fight pathogens by cutting off key metabolic pathways. This work is funded by the NIH.
(3) Bacterial oxidations that use O2 and can be used to convert renewable polymers and plastics to useful materials. Oxidations are a large class of reactions with vital applications in biotechnology and medicine. O2 is nature’s favorite chemically “green” oxidant: abundant, thermodynamically powerful, and, when properly, controlled, non-toxic. Typically, biological reactions begin by activating O2, using a protein-bound cofactor. Recently, we began work with a class of enzymes that accelerates reactions between O2 and organic substrates without the help of any cofactor. We are studying how these catalysts work on a fundamental level, and investigating applications of these and other bacterially mediated reactions to pressing environmental problems. The goal of this work is to use renewable strategies to carry out important bulk oxidation reactions, particularly the oxidative conversion of biological polymers and plastics to useful products. This work is being carried out in collaboration with the National Renewable Energy Lab and is funded by the National Science Foundation.
(4) Bacterial carboxylases that convert atmospheric CO2 to biomass. The most abundant enzyme on Earth, Rubisco, catalyzes the first step in the fixation of CO2 into biomass in green plants. We now know, however, that this is one of many processes in the biosphere in which CO2 is used as a carbon source. We are currently studying three microbial mechanisms for the fixation of CO2 or its hydrated counterpart, HCO3-. This work aims at developing an understanding of the many catalytic strategies by which nature makes use of carbon dioxide. This work is funded by the Department of Energy.
(5) Helping children learn, and learn to love, science. We are implementing a program for developing personally engaging STEM lessons for elementary and middle school students called “TAKE SHAPE”: Teaching Engineering and Science through Humor, the Arts, and Play. This program is funded in part by the National Science Foundation.
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.