Analysis of the order of free energy couplings between ligand binding and subunit assembly in human hemoglobin.
The concept of free energy couplings has been extensively used in studies of the ligand-linked subunit assembly of oligomeric proteins such as human hemoglobin A [cf. Ackers, G. K. (1980) Biophys. J. 32, 331-346]. Recently, the concept of "order" of free energy couplings has been introduced as a description of the number of protein subunits that must be liganded to effect changes in intersubunit interactions [Weber, G. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 7098-7102]. That report utilized the concept of order of free energy couplings to analyze a set of previously published equilibrium constants derived from data pertaining to the chemical equilibrium between oxygen and stripped hemoglobin A [Mills, F. C., Johnson, M. L., & Ackers, G. K. (1976) Biochemistry 15, 5350-5362]. The Weber report claims to have "unequivocally" demonstrated that the coupling between oxygenation and subunit assembly in hemoglobin A is "first order". In the present report, it is demonstrated that free energy couplings of both the first and second order are capable of describing the original oxygen binding data.
D006441:Hemoglobin A / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D046911:Macromolecular Substances; D008433:Mathematics; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics
D008024:Ligands; D046911:Macromolecular Substances; D006441:Hemoglobin A