Reversible conversion of nitroxyl anion to nitric oxide by superoxide dismutase

Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10860-4. doi: 10.1073/pnas.88.23.10860.

Abstract

Superoxide dismutase (SOD) rapidly scavenges superoxide (O2-) and also prolongs the vasorelaxant effects of nitric oxide (NO), thought to be the endothelium-derived relaxing factor. This prolongation has been ascribed to prevention of the reaction between O2- with NO. We report that SOD supports a reversible reduction of NO to NO-. When cyanamide and catalase were used to generate NO- in the presence of SOD, NO was measured by the conversion of HbO2 to MetHb. When SOD[Cu(I)] was exposed to NO anaerobically, NO- was trapped by MetHb forming nitrosylmyoglobin. When NO was generated by 3-morpholinosydnonimine hydrochloride in the presence of SOD, NO- or a similar reductant was formed, which reduced catalase compound II and promoted the formation of the catalase [Fe(III)]-NO complex. It is, therefore, conceivable that SOD may protect NO and endothelium-derived relaxing factor by a mechanism in addition to O2- scavenging and that NO- may be a physiologically important form of endothelium-derived relaxing factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalase / metabolism*
  • Cattle
  • Copper / pharmacology
  • Erythrocytes / enzymology
  • Free Radicals
  • Isoenzymes / blood
  • Isoenzymes / metabolism*
  • Kinetics
  • Liver / enzymology
  • Nitric Oxide / metabolism*
  • Nitrogen Oxides / metabolism*
  • Oxyhemoglobins / metabolism
  • Spectrophotometry
  • Superoxide Dismutase / blood
  • Superoxide Dismutase / metabolism*

Substances

  • Free Radicals
  • Isoenzymes
  • Nitrogen Oxides
  • Oxyhemoglobins
  • Nitric Oxide
  • Copper
  • Catalase
  • Superoxide Dismutase
  • nitroxyl