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http://dx.doi.org/10.5012/bkcs.2003.24.10.1470

Structural Dynamics of Myoglobin Probed by Femtosecond Infrared Spectroscopy of the Amide Band  

Kim, Seong-Heun (Department of Chemistry and Chemistry Institute for Funtional Materials, Pusan National University)
Jin, Geun-Young (Department of Chemistry and Chemistry Institute for Funtional Materials, Pusan National University)
Lim, Man-Ho (Department of Chemistry and Chemistry Institute for Funtional Materials, Pusan National University)
Publication Information
Bulletin of the Korean Chemical Society / v.24, no.10, 2003 , pp. 1470-1474 More about this Journal
Abstract
The dynamics of the tertiary conformation of myoglobin (Mb) after photolysis of carbon monoxide was investigated at 283 K solution by probing amide I and II bands using femtosecond IR absorption spectroscopy. Time-resolved spectra in the amide region evolve with 6-12 ps time scale without noticeable subpicosecond dynamics. The spectra measured at 100 ps delay after photolysis is similar to the difference FTIR spectrum at equilibrium. Time-resolved spectra of photoexcited Mb evolve modestly and their amplitudes are less than 8% of those of photolyzed MbCO, indicating that thermal contribution to the spectral evolution in the amide region is negligible. These observations suggest that the conformational relaxation ensuing photolysis of MbCO be complex and the final deoxy protein conformation have been substantially formed by 100 ps, probably with 6- 12 ps time constant.
Keywords
Conformational relaxation; Myoglobin; Femtosecond infrared spectroscopy; MbCO;
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