Kinetics and temperature dependence of carboxymyoglobin ligand photodissociation. Academic Article uri icon


  • 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.

published proceedings

  • Biophys J

author list (cited authors)

  • Reynolds, A. H., & Rentzepis, P. M.

citation count

  • 28

publication date

  • April 1982