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Related Experiment Videos

Interaction between nitric oxide and prostaglandin H synthase

A L Tsai1, C Wei, R J Kulmacz

  • 1Department of Internal Medicine, University of Texas Health Science Center at Houston 77030.

Archives of Biochemistry and Biophysics
|September 1, 1994
PubMed
Summary

Nitric oxide (NO) shows weak binding to resting Prostaglandin H synthase (PGHS) and minimal impact on its cyclooxygenase activity. This suggests no significant in vivo interaction between NO and PGHS.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Prostaglandin H synthase (PGHS) is a hemeprotein whose activity may be influenced by nitric oxide (NO).
  • Understanding the interaction between NO and PGHS is crucial for elucidating its physiological and pathological roles.

Purpose of the Study:

  • To investigate the interaction between nitric oxide (NO) and ovine Prostaglandin H synthase isoform-1 (PGHS-1).
  • To determine the effect of NO on PGHS activity and heme binding.

Main Methods:

  • Stopped-flow spectrophotometry was used to analyze NO binding kinetics to ferric PGHS.
  • Enzyme activity assays were performed on various PGHS preparations incubated with NO donors.

Main Results:

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  • Nitric oxide (NO) exhibited weak affinity for the heme in resting (ferric) PGHS, with an equilibrium dissociation constant (Kd) of 0.92 mM.
  • NO reacted strongly with ferrous PGHS under anaerobic conditions, displacing the histidine ligand.
  • Neither dissolved NO nor NO donors significantly decreased the cyclooxygenase activity of PGHS preparations.

    • Conclusions:

    • The direct interaction between NO and PGHS is weak at physiological concentrations.
    • NO does not significantly modulate the cyclooxygenase activity of PGHS.
    • These findings suggest limited in vivo modulation of PGHS by direct NO interaction.