| Abstract
| - Spectrally resolved three-pulse stimulated vibrational echo experiments are used as the basis for structuralassignments of the A1 and A3 spectroscopic substates in the IR spectrum of the carbon monoxide (CO) stretchof carbonmonoxymyoglobin (MbCO). The measured dephasing dynamics of these substates is compared tothe dephasing dynamics of MbCO predicted from molecular dynamics (MD) simulations. We assign the A1and A3 substates to different protein conformations on the basis of the agreement between the measured andcomputed vibrational echoes. In the A1 substate, the Nε−H proton and Nδ of His64 are equidistant from theligand, whereas in the A3 substate, the Nε−H of His64 is oriented toward the CO.
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