Molecular formula :
nature : vertebrates red blood cells in an iron compound mutant protein, and heme-globin combination. Its function is to transport oxygen and carbon dioxide to maintain blood acid-base balance. There are also low in certain animals and legume root nodules. About 67,000 molecular weight, containing over four peptide chains, each peptide chain containing a heme group, heme iron for the price of two, when combined with oxygen, and its price unchanged chemical form oxygenated hemoglobin. Bright red was, and after the dissociation of oxygen with a light blue. There are many types : A hemoglobin (HbA), α 2 β 2, accounting for adult hemoglobin of 98%; Hemoglobin A2 ( HbA2), α 2 δ 2, accounting for adult hemoglobin of 2%; F hemoglobin (HbF), α k2 γ 2, is the only fetal blood; hemoglobin H (HbH), β 4, the same four β chain of hemoglobin tetramer; blood red protein C (Therapy), β chain Glu Lys was replaced by hemoglobin; S hemoglobin (HbS), sickle-cell protein; hemoglobin O2 (HbO2 , HHbO2), oxyhemoglobin; hemoglobin CO (descending), the combination of carbon monoxide hemoglobin. In the absence of oxygen in the circumstances, the interaction between the four subunits of resilience. The more oxygen molecules of hemoglobin binding with the more intense. Center ion Fe (II) and further protein chain of histidine combined into five Coordination. Both distribution centers and is also active sites. Hemoglobin iron (II) can be reversible molecular oxygen combine depends on the oxygen partial pressure. It could from the alveolar oxygen partial pressure higher intake of oxygen and blood circulation with the release of oxygen partial pressure to lower tissue, and thus play a role in oxygen. Carbon monoxide and hemoglobin oxygen than the combination of strong, even in small concentrations can also combine priority and hemoglobin, causing the oxygen to flow interrupted, causing carbon monoxide poisoning.
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