Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient.

@article{Stamler1997BloodFR,
  title={Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient.},
  author={Jonathan S. Stamler and Li-ping Jia and Jerry P. Eu and Timothy J McMahon and Ivan T. Demchenko and Joseph Bonaventura and Kim Gernert and Claude A. Piantadosi},
  journal={Science},
  year={1997},
  volume={276 5321},
  pages={
          2034-7
        }
}
The binding of oxygen to heme irons in hemoglobin promotes the binding of nitric oxide (NO) to cysteinebeta93, 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… CONTINUE READING

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