Interaction of oxoferrylmyoglobin and dinitrosyl-iron complexes

Biochemistry (Mosc). 2004 May;69(5):569-74. doi: 10.1023/b:biry.0000029856.67884.c5.

Abstract

It is shown that dinitrosyl-iron complexes (DNIC) with glutathione can reduce oxoferrylmyoglobin forming on interaction of tert-butyl hydroperoxide and metmyoglobin. A rapid decrease in the DNIC concentration was observed under the conditions of production of tert-butyl free radicals; however, destruction of DNIC in the presence of oxoferrylmyoglobin alone was negligible. It is demonstrated that DNIC reduces oxoferrylmyoglobin more than an order more efficiently than S-nitrosoglutathione and glutathione. DNIC also inhibits formation of the thiyl radicals of glutathione in a medium containing metmyoglobin and tert-butyl hydroperoxide. A mechanism of the antioxidant action of DNIC based on regeneration of the nitrosyl complexes from the products of their interaction with oxoferrylheme is proposed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antioxidants / metabolism
  • Cyclic N-Oxides / metabolism
  • Electron Spin Resonance Spectroscopy
  • Free Radicals / metabolism
  • Glutathione / metabolism
  • Iron / metabolism*
  • Metmyoglobin / metabolism*
  • Nitric Oxide
  • Nitrogen Oxides / metabolism*
  • S-Nitrosoglutathione / metabolism
  • tert-Butylhydroperoxide / metabolism

Substances

  • Antioxidants
  • Cyclic N-Oxides
  • Free Radicals
  • Nitrogen Oxides
  • ferrylmyoglobin
  • Metmyoglobin
  • 5-diethoxyphosphoryl-5-methyl-1-pyrroline N-oxide
  • Nitric Oxide
  • S-Nitrosoglutathione
  • dinitrosyl iron complex
  • tert-Butylhydroperoxide
  • Iron
  • Glutathione