Kinetics and temperature dependence of carboxymyoglobin ligand photodissociation.
We have observed the rate of oxymyoglobin (MbO2) photodissociation at room temperature and carboxymyoglobin (MbCO) photodissociation as a function of temperature (260-10 K) by means of picosecond spectroscopy. The Mb + O2 and Mb + CO photodissociated states have also been characterized. Based on the picosecond experimental data, we postulate that the photodissociation  of ligated myoglobin is a nonactivitated process, and the mechanism involves either a small enthalpy barrier or none at all.
D000818:Animals; D002248:Carbon Monoxide; D007700:Kinetics; D008024:Ligands; D009211:Myoglobin; D010782:Photolysis; D013696:Temperature; D013816:Thermodynamics; D014907:Whales
D008024:Ligands; D009211:Myoglobin; C018013:carboxymyoglobin; D002248:Carbon Monoxide