Hemoglobin dioxygen binding

Spin-pairing model of dioxygen binding and its application to various transition metal systems as well as hemoglobin cooperativity. R. S. Drago and B. B. Corden, Acc. Chem. Res., 1980, 13, 353-360 (39). 

Hemoglobin s dioxygen binding is regulated by local concentrations of H+ (known as the Bohr effect), CO2 concentration, and organic phosphates such as diphosphoglycerate (DPG), whose structure is shown in Figure 4.2.17... 

Figure 4.9 Dioxygen binding curves for myoglobin and hemoglobin. (Reprinted with permission from Figure 4.4 of Cowan, J. A. Inorganic Biochemistry, An Introduction, 2nd ed., Wiley-VCH, New York, 1997. Copyright 1997, Wiley-VCH.)...

Fig. 19.9 Dioxygen binding curves for (I) myoglobin and for hemoglobin at various partial pressures of carbon dioxide (2) 20 mm Hg (3) 40 mm Hg (4) 80 mm Hg. Note that myoglobin has a stronger affinity for dioxygen than hemoglobin and that this effect is more pronounced in the presence of large amounts of carbon dioxide. [Modified from Bock. A. V. Field, H., Jr. Adair. G. S. J. Biol. Chem. 1924. 59, 353-378. Reproduced with permission.)...

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