Irving S. Sigal Postdoctoral Fellowship - Current Recipient

Dr. Lisa Olshansky

American Chemical Society Awards Eleventh Irving S. Sigal Postdoctoral Fellowship

The American Chemical Society, the world’s largest scientific society, has awarded the 11th Irving S. Sigal Postdoctoral Fellowship (2016-2018) to Dr. Lisa Olshansky.

Lisa completed her doctoral studies in 2015, under the supervision of Professor Daniel G. Nocera at Massachusetts Institute of Technology.  Lisa’s postdoctoral research will be on “Artificial Metalloenzymes for Structure-Function Correlations of C–H Bond Oxidation”, under the supervision of Professor A. S. Borovik at University of California, Irvine.

Lisa’s doctoral dissertation is titled “Kinetics and Dynamics Controlling Proton-Coupled Electron Transfer in Ribonucleotide Reductase”.  Her doctoral research focused on the study of proton-coupled electron transfer, a fundamental mechanism serving as the basis for biological energy transduction, as well as biosynthetic and signaling processes.

For her Irving S. Sigal Postdoctoral Fellowship, Lisa will investigate how nature controls the reactivity of metallocofactor intermediates for the oxidation of strong chemical bonds. Oxidation reactions performed by metalloenzymes maintain specificity and catalytic efficiencies not yet matched by synthetic systems and the general understanding of how nature harnesses the energy of O–O bond homolysis for C–H bond functionalization remains incomplete.  The proposed studies by Lisa aim to reveal the underlying structure-function (and dysfunction) relationships operative within oxygenase metalloenzymes that are critical to metabolic and signaling pathways, and in the management of reactive oxygen species. These questions will be probed through the preparation of artificial metalloproteins in which the host-guest interaction of streptavidin and biotin is used to insert biotinylated metal complexes into the protein interior. Combining chemical modulation of the ligand scaffold with genetic modification of the surrounding protein microenvironment, the ability to control and systematically vary all aspects of the metal ion coordination sphere will be achieved. These studies represent a method with which to prepare novel biomimetic systems and a means to correlate the structure-function paradigms underlying bioinorganic oxygenase reactivity.