Hemoglobin the iron gets recycled. This process also produces one molecule of carbon monoxide for every molecule of heme degraded. Heme degradation is one of the few natural sources of carbon monoxide in the human body, and is responsible for the normal blood levels of carbon monoxide even in people breathing pure air. The other major final product of heme degradation is bilirubin. Increased levels of this chemical are detected in the blood if red blood cells are being destroyed more rapidly than usual. Improperly degraded hemoglobin protein or hemoglobin that has been released from the blood cells too rapidly can
Oxygen–hemoglobin dissociation curve formation of methemoglobin and superoxide, O, instead of the usual products. Superoxide is a free radical and causes biochemical damage, but is neutralised by the action of the enzyme superoxide dismutase. Myo-inositol trispyrophosphate (ITPP), also known as OXY111A, is an inositol phosphate that causes a rightward shift in the oxygen hemoglobin dissociation curve through allosteric modulation of hemoglobin within red blood cells. It is an experimental drug intended to reduce tissue hypoxia. The effects appear to last roughly as long as the affected red blood cells remain in circulation. Fetal hemoglobin (HbF) is structurally different from normal adult hemoglobin (HbA),