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Updated: Aug 13, 2026

Analytical Techniques for Assaying Nitric Oxide Bioactivity
Published on: June 18, 2012
Nitric oxide binding to oxygenated hemoglobin under physiological conditions
Z Huang1, J G Louderback, M Goyal
1Department of Physics, Wake Forest University, Winston-Salem, NC 27109-7507, USA.
Abstract:
We have added nitric oxide (NO) to hemoglobin in 0.1 M and 0.01 M phosphate buffers as well as to whole blood, all as a function of hemoglobin oxygen saturation. We found that in all these conditions, the amount of nitrosyl hemoglobin (HbNO) formed follows a model where the rates of HbNO formation and methemoglobin (metHb) formation (via hemoglobin oxidation) are independent of oxygen saturation. These results contradict those of an earlier report where, at least in 0.01 M phosphate, an elevated amount of HbNO was formed at high oxygen saturations. A radical rethink of the reaction of oxyhemoglobin with NO under physiological conditions was called for based on this previous proposition that the primary product is HbNO rather than metHb and nitrate. Our results indicate that no such radical rethink is called for.
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