The effects of pressure on oxygen and carbon monoxide binding kinetics for myoglobin. A high pressure laser flash photolysis study.

The milli-, micro-, and nanosecond rebinding kinetics of oxygen and carbon monoxide with myoglobin (Mb) from sperm whale, horse, and dog were studied as a function of pressure up to 2 kbar by means of a high pressure laser photolysis apparatus. The results were analyzed quantitatively in terms of a three-step reaction scheme, and activation volumes (delta V not equal to) for each step were determined from the pressure dependence of the rate constants. In the case of CO binding to Mb, the overall reaction volume delta V not equal to was negative, resulting from the rate-determining bond formation step. Activation volumes for O2 to the iron binding step as well as for the O2 diffusion step within the protein matrix were quite different among three Mb species, and it was suggested that activation volumes are very sensitive to the amino acid constituents around the ligand path channel.