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| Type |
Poster Presentation |
| Area |
물리화학 |
| Room No. |
포스터발표장 |
| Time |
4월 20일 (목요일) 11:00~12:30 |
| Code |
PHYS.P-40 |
| Subject |
Conformation-dependent Rebinding Dynamics of CO with Myoglobin Investigated by Time-resolved Infrared Spectroscopy |
| Authors |
신주향, 임만호*, 박성철
부산대학교 화학과, Korea
|
| Abstract |
Myoglobin is one of the simplest heme proteins and has been studied extensively using a variety of physical techniques. In this study, we have measured the ground state bleaching of MbCO at low pH using time-resolved vibrational spectroscopy. When excited with a 532-nm photon, carbon monoxide dissociated immediately from myoglobin (< 0.2 ps), ground state bleaching of CO bound to the myoglobin has three conformations (A0, A1 and A3). Each conformation shows characteristic 13C−O stretching frequencies : 1920 cm-1 for A0, 1990 cm-1 for A1 and 1896 cm-1 for A3. Ligand binding to myoglobin is a multiphasic process with fast geminate rebinding arising on the nanosecond timescales and slower bimolecular rebinding occurring on microsecond timescales.We have observed faster geminate rebinding time and bimolecular rebinding time for A0 than the others. |
| E-mail |
dksvmflzk@gmail.com |
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119th General Meeting of the KCS