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Biophysical Journal 57: 369-373 (1990)
© 1990 the Biophysical Society
AT&T Bell Laboratories, Murray Hill, New Jersey 07974.
ABSTRACT
Time-resolved infrared spectroscopy with 0.5-ps resolution is used to track the evolution of the CO stretching vibration after visible photoexcitation of carboxyhemoglobin in water at room temperature. Polarization measurements determine that the iron-complexed CO is oriented nearly perpendicular to the porphyrin plane. The dissociation appears to proceed via a metastable excited state with 2 +/- 1 ps lifetime. The dissociated CO binds weakly in the heme pocket for at least 500 ps. This state correlates with the internally bound state observed by Frauenfelder et al. at low temperatures in myoglobin.
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