Functional and spectroscopic evidence for a conformational transition in ferrous liganded human hemoglobin.

The effect of pH and/or organic phosphate on the kinetics of O2 dissociation from oxygenated human hemoglobin and on the spectroscopic features shown by the ferrous nitrosylated derivative of human hemoglobin has been investigated. The results indicate the occurrence of conformational change(s) taking place in liganded ferrous hemoglobin, bringing about a faster kinetic ligand dissociation process, accompanied by the appearance of peculiar spectroscopic features of the ferrous nitrosylated hemoglobin. Altogether these functional and spectroscopic observations indicate the existence of a nesting of tertiary and/or quaternary conformations in the liganded forms of human hemoglobin which may account for the action of heterotropic effectors, such as protons and organic phosphates.