Hemoglobin by molecules such as carbon monoxide (for example, from tobacco smoking, exhaust gas, and incomplete combustion in furnaces). CO competes with oxygen at the heme binding site. Hemoglobin's binding affinity for CO is 250 times greater than its affinity for oxygen, meaning that small amounts of CO dramatically reduce hemoglobin's ability to transport oxygen. Since carbon monoxide is a colorless, odorless and tasteless gas, and poses a potentially fatal threat, carbon monoxide detectors have become commercially available to warn of dangerous levels in residences. When hemoglobin combines with CO, it forms a very bright red compound called carboxyhemoglobin, which may
Hemoglobin Hopkins-2 carboxyl group of the amino acid forms a hydrogen bond with phenolix hydroxyl, which in turn stabilizes the structure of the molecule and increases oxygen affinity. Ho-2 hemoglobin has high levels of oxygen, which replaces the lack of oxygen within red blood cells. Ho-2 is similar to Hemoglobin A, which is normal hemoglobin and also contains two α-chains. This provides an explanation as to how the Hopkins-2 variant of hemoglobin is related to the symptoms of sickle cell. Hopkins-2 can also interact specifically with Hemoglobin S. Hemoglobin S is the most common abnormal hemoglobin variant. Hemoglobin S is the variant