Contact information
Tel: (office) +82-42-350-2819, (lab) +82-42-350-2859
Location: (office) Room 1104 (Bldg. E6-4), (lab) Room 1116, 1117 (Bldg. E6-4)
Fax: +82-42-350-2810
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
RESEARCH AREA
Brief Introduction
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
Representative publications
“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.
