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Blood Flow Regulation by S-Nitrosohemoglobin in the Physiological Oxygen Gradient

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Science  27 Jun 1997:
Vol. 276, Issue 5321, pp. 2034-2037
DOI: 10.1126/science.276.5321.2034

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Abstract

The binding of oxygen to heme irons in hemoglobin promotes the binding of nitric oxide (NO) to cysteineβ93, formingS-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.

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