Ps infrared vibrational echo experiments on myoglobin and myoglobin mutants
are presented. The vibrational dephasing experiments examine the influence
of protein dynamics on the CO ligand, at the active site of myoglobin, fro
m low temperature to physiologically relevant temperatures. The vibrational
echo results are combined with measurements of the CO vibrational lifetime
to yield the homogeneous pure dephasing. The pure dephasing is the Fourier
transform of the homogeneous linewidth with the lifetime contribution remo
ved. The mutant H64V protein's CO vibrational pure dephasing rate is simila
r to 20% slower (narrower pure dephasing linewidth) than the native protein
at all temperatures, although the only difference between the two proteins
is the replacement of the native's polar distal histidine by a non-polar v
aline. The mutant H93G(N-MeIm) pure dephasing is identical to the native's,
despite the severing of the only covalent bond between the heme and the gl
obin. These results provide insights into the mechanisms of the transmissio
n of protein fluctuations to the CO ligand bound at the active site.