Nitric oxide donors activate the cyclo-oxygenase and peroxidase activities of prostaglandin H synthase

Mauro Maccarrone, Sabrina Putti, Alessandro Finazzi Agrò

Research output: Contribution to journalArticlepeer-review

Abstract

Prostaglandin H synthase (PHS) is a dual enzyme with cyclo-oxygenase and peroxidase activities. The nitric oxide (NO) donors, sodium nitroprusside (SNP), S-nitroso-N-acetyl-penicillamine (SNAP) and spermine NONOate (SPER/NO), activated both cyclo-oxygenase and peroxidase activities of PHS. SNP activated PHS by increasing V(max) without affecting K(m), the activation constants being 1.0 mM for cyclo-oxygenase and 1.3 mM for peroxidase. Analysis of progress curves and absorption spectra of PHS suggested that NO released from SNP interacted with the heme at the active site of the enzyme. Moreover, SNP counteracted the peroxide-induced inactivation of PHS, suggesting that the interplay between the intracellular peroxide and NO is critical in tuning PHS activity in cells.

Original languageEnglish
Pages (from-to)470-476
Number of pages7
JournalFEBS Letters
Volume410
Issue number2-3
DOIs
Publication statusPublished - Jun 30 1997

Keywords

  • Arachidonate cascade
  • Cyclo-oxygenase
  • Nitric oxide
  • Peroxidase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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