Mentor: Dr. Leslie Murray
College of Liberal Arts and Sciences
"In my first semester I wanted to choose between my main interests in chemistry and languages and literature, so I joined a research group to get an idea of what I career in chemistry might be like. I soon found that I enjoyed the unique challenges and rewards of novel research work and decided to continue with it in preparation for a future career."
- Inorganic synthesis
- Small molecule activation
- Bioinorganic chemistry
- 2012-2016 National Merit Scholar
- 2014 Anderson Scholar
- 2015 UC Berkeley Amgen Scholar
Hobbies and Interests
Small Molecule Activation by Designed Triiron Complexes
In the biosphere, difficult multielectron redox transformations are accomplished under ambient conditions by enzymes with multimetallic active sites, such as the iron-molybdenum cofactor found in some variants of nitrogenase. The protein scaffold in these enzymes dictates the geometry of the active site and controls the relative disposition of the metal centers to favor cooperative reactivity. This metal-metal cooperativity facilitates substrate binding and activation by concerted transfer of multiple electrons to or from the substrate. Additionally, the protein fold can enforce low-coordinate geometries around the metal centers, increasing their reactivity, while simultaneously tuning the size and shape of the active site, thereby increasing selectivity toward the desired substrate. Developing methods to efficiently conduct the reactions catalyzed by these enzymes is one of the most significant challenges in synthetic chemistry. Consequently, this work aims to apply the design principles found in such enzymes to the synthesis of well-defined triiron complexes capable of performing cooperative small molecule activation, such as in the reduction of dinitrogen.