Nitric oxide (NO•), the only nitrogen monoxide redox form capable of activating soluble guanylyl cyclase

doi:10.1016/0006-2952(96)00078-0

Biochemical Pharmacology

Volume 51, Issue 12, 28 June 1996, Pages 1593-1600

https://doi.org/10.1016/0006-2952(96)00078-0 Get rights and content

Abstract

In the present study, we determined that of the redox forms of nitrogen monoxide, NO⁻, NO^• and NO⁺, only NO^. significantly activates soluble guanylyl cyclase (GTP pyrophosphate-lyase cyclizing, EC 4.6.1.2). Neither of the NO⁻ donors tested, Angeli's salt (Na₂N₂O₃) or Piloty's acid (C₆H₅SO₂NHOH), caused a change in the guanylyl cyclase activity relative to the basal activity level. Interference by other reaction products was eliminated as a possible explanation for the lack of activation. To the extent that NO⁺ could be stabilized in aqueous solution, by dissolution of the nitrosonium salt NOPF₆ in dry organic solvent prior to addition to the enzyme in buffer, NO⁺ had no effect on the activity of soluble guanylyl cyclase. The counter-ion, PF₆⁻, had a minimal effect on the enzyme activity and, therefore was, not responsible for the lack of activation by NO⁺. These observations suggest that NO^. is the natural activator of soluble guanylyl cyclase and is reasonably identical with endothelium-derived relaxing factor, the physiological regulator of soluble guanylyl cyclase activity.

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^☆: This research was supported by a Grant-in-Aid from the American Heart Association. E.A.D. gratefully acknowledges support of the NIH Biotechnology Training Grant.

^∗: In partial fulfillment of the requirements for the Ph.D., June 1995.

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Research paperNitric oxide (NO•), the only nitrogen monoxide redox form capable of activating soluble guanylyl cyclase☆

Abstract

J Biol Chem

Biochem Biophys Acta

J Biol Chem

J Biol Chem

FEBS Lett

J Biol Chem

Biochem Biophys Res Commun

Trends Biol Sci

J Biol Chem

Biochem Pharmacol

J Biol Chem

Biochem Biophys Res Commun

Eur J Pharmacol

Biochem Biophys Res Commun

J Biol Chem

Coordin Chem Rev

Inorg Chim Acta

Biochim Biophys Acta

J Biol Chem

J Biol Chem

Biochem Biophys Res Commun

Heme-dependent activation of soluble guanylate cyclase by nitric oxide: Regulation of enzyme activity by porphyrins and metalloporphyrins

Semin Hematol

Soluble guanylyl cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states

Biochemistry

Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): Characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme

Biochemistry

Resonance Raman spectroscopy of soluble guanylyl cyclase reveals displacement of distal and proximal heme ligands by NO

J Am Chem Soc

Research paper
Nitric oxide (NO^•), the only nitrogen monoxide redox form capable of activating soluble guanylyl cyclase☆