Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin.
The temporal shift in the near-IR absorption peak of myoglobin (Mb) following flash photolysis of MbCO at cryogenic temperatures appears to be due largely to an inhomogeneous reactive process rather than to relaxation. This conclusion, which follows from a new analysis of the experimental data, is based on the following three points: First, at very low temperatures (60 K) a transient line-narrowing effect can be detected. Second, there is a universal, temperature-independent, correlation between spectral shift and survival probability in the rebinding kinetics, and third, the same quantitative model which accounts for rebinding accounts semiquantitatively for the temporal shift in the peak. A fit to the model indicates that the inhomogeneous broadening of the near-IR peak in myoglobin is 15-20% of the total width. The same rebinding process which governs the loss of intensity of this peak is therefore most likely responsible for the shift in its center wavelength.
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Department of Physical Chemistry, Hebrew University, Jerusalem, Israel.
D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism*; D005615:Freezing; D007700:Kinetics; D009211:Myoglobin / Q000378:metabolism*; D010782:Photolysis; D011485:Protein Binding; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D014907:Whales
D009211:Myoglobin; C018013:carboxymyoglobin; D002248:Carbon Monoxide