Quaternary structure of partially liganded intermediates of sheep carbon monoxide hemoglobin at alkaline pH.
A rapid change in absorbance was observed in the Soret region during the interval between photolysis of sheep carbon monoxide hemoglobin and the subsequent reassociation of CO in the dark. The rate constant for this spectral change was about 4000 s--1 at 20 degrees in 0.05 M solium borate, pH 9.3. The wavelength dependence of the amplitude of the absorbance change is similar to that observed when deoxygenated alpha and theta chains are allowed to recombine (Brunori, M., Antonini, E., Wyman, J., and Anderson, S. R. (1968) J. Mol. Biol. 34, 357-359), and therefore reflects changes in the quanternary structure of the hemoglobin tetramer induced by ligand displacement. The amplitude of this conformation-dependent spectral change was not a linear function of the fraction of bound CO removed by photolysis. The results suggest that of the possible intermediate species present after partial photolysis, only Hb4 and Hb4(CO) change from the ligand-bound to the ligand-free sturcture prior to CO reassociation under these alkaline conditions.
D000818:Animals; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; D006454:Hemoglobins; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D010108:Oxyhemoglobins; D011485:Protein Binding; D012756:Sheep
D006454:Hemoglobins; D008024:Ligands; D010108:Oxyhemoglobins; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin