The Rates of Combination of the Isolated Chains of Human Hemoglobin with Oxygen

The rates of combination of the isolated chains of human hemoglobin with oxygen have been measured by flash photolysis and stopped flow methods. The two experimental methods give similar results, and furthermore the data compare well with those obtained recently by the temperature jump relaxation method. The measured association rates are compared with the values predicted from the previously measured equilibrium and dissociation rate constants. A significant discrepancy is noted in the case of the : chains. In addition, the rates of replacement of oxygen by carbon monoxide as functions of the relative ligand concentrations have been measured, and the observed dependences are compared to those predicted from the equilibrium and kinetic constants for the individual liganding reactions.