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Related Experiment Videos

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.

Biochimica Et Biophysica Acta
|January 12, 2002
PubMed
Summary

Nitric oxide (NO) reacts with hemoglobin (Hb) forming nitrosyl hemoglobin (HbNO) and methemoglobin (metHb). Our findings show HbNO and metHb formation rates are independent of oxygen saturation, contradicting prior research.

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Area of Science:

  • Biochemistry
  • Physiological Chemistry

Background:

  • Nitric oxide (NO) plays a crucial role in various physiological processes.
  • The reaction between NO and hemoglobin (Hb) is critical for understanding NO bioavailability and its effects.
  • Previous studies proposed that NO preferentially forms nitrosyl hemoglobin (HbNO) over methemoglobin (metHb) at high oxygen saturation.

Purpose of the Study:

  • To investigate the formation of HbNO and methemoglobin (metHb) when NO is added to hemoglobin under varying oxygen saturation levels.
  • To determine if oxygen saturation influences the reaction kinetics of NO with hemoglobin.
  • To re-evaluate previous findings on the reaction products of oxyhemoglobin with NO.

Main Methods:

  • Addition of nitric oxide (NO) to hemoglobin solutions in phosphate buffers (0.1 M and 0.01 M) and to whole blood.

Related Experiment Videos

  • Systematic variation of hemoglobin oxygen saturation levels.
  • Quantification of nitrosyl hemoglobin (HbNO) and methemoglobin (metHb) formation.

    • Main Results:

    • The formation of both HbNO and methemoglobin (metHb) proceeded at rates independent of hemoglobin oxygen saturation across all tested conditions.
    • These findings were consistent in phosphate buffers and whole blood.
    • The observed kinetics contradict a previous report suggesting elevated HbNO formation at high oxygen saturation.

    Conclusions:

    • The reaction kinetics of NO with hemoglobin, leading to HbNO and metHb formation, are not significantly influenced by oxygen saturation.
    • The previously proposed model requiring a "radical rethink" of NO-hemoglobin interactions under physiological conditions is not supported by these results.
    • The formation of methemoglobin and nitrosyl hemoglobin occurs independently of oxygen saturation levels.