Studies on ligand binding to sulphaemoglobin.
Equilibrium studies show that, at low protein concentrations, sulphaemoglobin, in the ferrous form, binds carbon monoxide at pH 6.0 in a non co-operative manner with a Hill coefficient of 1.15 and an affinity constant of 8 . 10(-7) M. At both pH 6.0 and pH 9.0 the kinetics of CO binding show the presence of a simple mono-exponential process with a second-order rate constant of 8 . 10(3) M-1 . s-1. The rate of dissociation of CO from sulphaemoglobin is approx. 0.01 s-1. The activation energy of the binding process is calculated as 40 kJ . mol-1. A comparison is presented between the CO binding properties of sulphaemoglobin, myoglobin and haemoglobin and a mechanism whereby the CO binding parameters of sulphaemoglobin are modified is proposed.
D002248:Carbon Monoxide / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009211:Myoglobin / Q000378:metabolism; D011485:Protein Binding; D013435:Sulfhemoglobin / Q000378:metabolism*
D006454:Hemoglobins; D009211:Myoglobin; D002248:Carbon Monoxide; D013435:Sulfhemoglobin