Education Ph. D. Chemistry, University of Wisconsin-Madison, May, 2010(Graduate Advisor: Prof. Thomas C. Brunold) B. S. Chemistry, Seoul National University, February, 2004 Career Assistant Professor, Department of Chemistry, KAIST 2014 - present· Postdoctoral fellow (Prof. Edward I. Solomon) 2010 - 2014 Department of Chemistry, Stanford University· Graduate Research Assistant (Prof. Thomas C. Brunold) 2006 - 2010 Department of Chemistry, University of Wisconsin-Madison

Physical Chemistry and Bioinorganic chemistry

More than one third of enzymes are metalloenzymes and a majority of industrial catalysts are organometallic compounds. To understand their reaction mechanisms and thus to have control over their reactivity, we need specialized tools to probe the metal centers selectively and directly. Using spectroscopic techniques, such as magnetic circular dichroism, electron paramagnetic resonance, and nuclear resonance vibrational spectroscopy, in combination with quantum chemical calculations, we define the electronic and geometric structures of key reaction intermediates and correlate them to their catalytic function and reactivity. Systems of our interest encompass bio-inspired proton reduction and water oxidation catalysts, organometallic catalysts, and metal-based drugs Research topics Transition-metal-containing catalysts Electronic and geometric structures of reaction intermediates Magnetic Circular Dichroism Electron Paramagnetic Resonance Nuclear Resonance Vibrational Spectroscopy Density Functional Theory computations

“Nuclear Resonance Vibrational Spectroscopic and Computational Study of High-valent Diiron Complexes Relevant to Enzyme Intermediates”, Proc. Natl. Acad. Sci. USA, 2013, 110, 6275-6280. “Nuclear Resonance Vibrational Spectroscopy and DFT Study of Peroxo-bridged Biferric Complexes: Structural Insight into Peroxy Intermediates of Binuclear Non-heme Iron Enzymes”, Angew. Chem. Int. Ed. 2013, 52, 1294-1298. “Resonance Raman and Computational Studies of B12 cofactors”, J. Phys. Chem. B, 2013, 117, 5397-5410.

“Spectroscopic Characterization of Active-Site Variants of the PduO-type ATP:Corrinoid Adenosyltransferase from Lactobacillus reuteri: Insights into the Mechanism of Four-Coordinate Co(II)corrinoid Formation”, Inorg. Chem. 2012, 51, 4482-4494.