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| Type |
Symposium |
| Area |
Recent Trends in Bio-Inorganic Chemistry |
| Room No. |
Room 211+212+213 |
| Time |
FRI 09:00-: |
| Code |
INOR1-1 |
| Subject |
Charge transfer as key principles of C-H bond activation and cross coupling |
| Authors |
Kiyoung Park
Department of Chemistry, Korea Advanced Institute of Science and Technology, Korea |
| Abstract |
Metalloenzymes and metallocofactors in nature often demonstrate uniquely high efficiency that cannot be observed elsewhere. One example is C-H bond activation by non-heme iron enzymes; mononuclear or binuclear iron sites utilize O2 to form high-valent intermediates that can abstract H atom from strong bonds such as the C-H bond of methane. The principle of these reactions has been elucidated on the basis of intermediate structures established by nuclear resonance vibrational spectroscopy, revealing that spin-polarized charge transfer from oxo ligand to Fe center determines intrinsic barrier for the reaction.
A series of high-valent organometallic complexes that show different rates of reductive elimination process have been spectroscopically and computationally studied. A good correlation amongst the energy level of redox-active metal d orbitals, the type of supporting ligands, and cross coupling reaction rate demonstrate that the activity and selectivity of C-C bond cross coupling reaction can be understood in parallel with enzyme’s strategy to raise the reduction potential of a metal center by dissociating or exchanging ligands.
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| E-mail |
kiyoung.park@kaist.ac.kr |
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120th General Meeting of the KCS