Hemoglobin (Hb) is the O2-carrying protein in our blood. Unlike myoglobin, it has four sites allowing it to bind up to four O2 m
olecules. Additionally, the tendency of O2 to bind to each site increases as the other three sites become occupied (this is an example of a phenomenon known as positive cooperativity). To model this effect, consider a simplified hemoglobin-like protein with two binding sites. When no sites are occupied, the system energy is 0; when only one of the two sites is occupied, the energy is E; and when both sites are occupied, the energy is 2E J. Here J parameterizes the cooperativity, as when both sites are occupied, the energy is not simply the sum of the individual binding energies at each site.
Yes, the energy is not simply the sum of the individual binding energies at each site, it is the product of energy at each binding site of hemoglobin.
Explanation:
Myoglobin and hemoglobin are two different cells. Myoglobin binds only one oxygen while the hemoglobin has the ability to binds four oxygen atoms at its four sides. Myoglobin present in muscle tissue only while hemoglobin is present in the whole body. Oxyhemoglobin is formed when oxygen binds with hemoglobin cell. This oxygen is take to all cells and energy is released due to the breakdown of glucose molecules with this oxygen.
