Sponsor: Alfred R. Bader Fund
Citation: For developing spectroscopic methods and defining electronic structure contributions to function in electron transfer and dioxygen activation and reduction by copper and iron metalloenzymes.
Current position: Monroe E. Spaght Professor of Chemistry, Stanford University; professor of photon science, SLAC National Accelerator Laboratory
Education: B.S., chemistry, Rensselaer Polytechnic Institute; Ph.D., chemistry, Princeton University
Solomon on his current scientific goals: “I want to understand the general principles of O2 activation by Cu and Fe metalloenzyme active sites and how these relate to parallel active sites in heterogeneous and homogeneous catalysis. Also how the iron-oxo intermediates in heme enzymes relate to those in nonheme iron enzymes and how the different active sites used by nature in the reduction of O2 to water enable their oxidase versus proton pumping functions.”
What his colleagues say: “Ed Solomon has enormously impacted the depth, breadth, and eminence of bioinorganic chemistry by bringing spectroscopic methods and electronic structural-bonding insights to both protein-metal and synthetic model chemistries of numerous other research groups.”—Kenneth Karlin, Johns Hopkins University