Cooperative Oxygen Binding with Hemoglobin as a General Model in Molecular Biophysics

Studies of hemoglobin and its oxygenation and thermodynamic and mathematical models developed for the purpose allowed substantial advances in biophysics, and equations derived in the field and, in particular, the Hill equation influenced the development of science in many other fields. Hemoglobin and its allosteric mechanism regulating the binding of oxygen and other ligands served as a model of a huge number of molecular biological systems. The review focuses on the formal description of oxygen binding by hemoglobin and considers the main mathematical models developed in this area. Evolution of binding models is tracked from the approaches proposed by Hill, Adair, Monod–Wyman–Changeux, and Koshland–Némethy–Filmer to modern views. Particular attention is paid to various formal approaches and ideas used to describe oxygenation as a phenomenon of physical adsorption.