Abstract

The binding of oxygen to heme irons in hemoglobin promotes the binding of nitric oxide (NO) to cysteineβ93, forming S -nitrosohemoglobin. Deoxygenation is accompanied by an allosteric transition in S -nitrosohemoglobin [from the R (oxygenated) to the T (deoxygenated) structure] that releases the NO group. S -nitrosohemoglobin contracts blood vessels and decreases cerebral perfusion in the R structure and relaxes vessels to improve blood flow in the T structure. By thus sensing the physiological oxygen gradient in tissues, hemoglobin exploits conformation-associated changes in the position of cysteineβ93 SNO to bring local blood flow into line with oxygen requirements.