Montana State University
Department of Chemistry and Biochemistry
224 Chemistry and Biochemistry & Building
Bozeman, MT 59717
Nitrogenase is a two-component metalloenzyme that catalyzes the MgATP-dependent reduction of N2 to yield 2 molecules of NH3, a process otherwise known as biological nitrogen fixation. I am investigating the structural and functional properties of nitrogenases from Azotobacter vinelandii, a soil bacterium that is able to fix nitrogen aerobically while protecting the oxygen-sensitive nitrogenase enzymes. A. vinelandii can produce three different nitrogenase enzymes depending on metal availability: the most common and widely studied being molybdenum nitrogenase and the other two alternative nitrogenases are vanadium nitrogenase and iron nitrogenase.
The remarkable ability of this enzyme overcome the large energy activation barrier to fix N2, has enabled the discovery of other substrates for nitrogenase such as CO2 and CO. Wild-type molybdenum nitrogenase can reduce N2 more efficiently whereas the alternative vanadium nitrogenase has been found to reduce carbon substrates such as CO2 to CH4, a renewable fuel. The goal is to discover the differences between these homologous nitrogenase enzymes that enable the reduction of diverse carbon and nitrogen-substrates to produce products that have wide applications in biofuel production and agriculture.
I grew up in Orofino, ID and received a bachelor’s degree in chemistry in 2009 from the College of Idaho. After graduating, I worked as a Post-Bachelor’s Research Associate at Pacific Northwest National Laboratory for a year before moving to Bozeman, MT. I joined the Peters’ Lab in January 2015. I love the mountains and snowboarding so this is the perfect place for me!