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
Glycated hemoglobin the degree of control of glucose metabolism in diabetic patients was proposed in 1976 by Anthony Cerami, Ronald Koenig and coworkers. Glycated hemoglobin causes an increase of highly reactive free radicals inside blood cells. Radicals alter blood cell membrane properties. This leads to blood cell aggregation and increased blood viscosity which results in impaired blood flow. Another way glycated Hb causes damage is via inflammation which results in atherosclerotic plaque (atheroma) formation. Free radical build-up promotes the excitation of Fe-Hb through into abnormal ferryl Hb (Fe-Hb). Fe is unstable and reacts with specific amino acids in Hb to regain its