Vibrational Dynamics of Carbon Monoxide at the Active Sites of Mutant Heme Proteins

@inproceedings{HillVibrationalDO,
  title={Vibrational Dynamics of Carbon Monoxide at the Active Sites of Mutant Heme Proteins},
  author={Jeffrey R. Hill and Dana D. Dlott and Kristen A. Peterson and Sean M. Decatur and Steven G Boxer and Michael D Fayer}
}
Picosecond mid-IR pump -probe measurements of vibrational relaxation (VR) of CO bound to the active sites of wild-type and mutant myoglobins (Mb) reveal that an approximately linear relationship exists between the protein matrix-induced CO frequency shift and the VR rate. This relation parallels a similar linear relationship seen in a series of heme model compounds where Fe was replaced by Ru and Os. The VR rate of CO in the Mb is sensitive only to the magnitude of protein-induced carbonyl… CONTINUE READING
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