Oxidation of cyanide to the cyanyl radical by peroxidase/H2O2 systems as determined by spin trapping.
The cyanyl radical was formed during the oxidation of potassium or sodium cyanide by horseradish peroxidase, lactoperoxidase, chloroperoxidase, NADH peroxidase, or methemoglobin in the presence of hydrogen peroxide. The spin adducts of the cyanyl radical with 5,5-dimethyl-1-pyrroline-N-oxide and N-tert-butyl-alpha-phenylnitrone were quite stable at neutral pH. The identity of these spin adducts could be demonstrated using 13C-labeled cyanide and by comparison with the spin adducts of the formamide radical, a hydrolysis product of the cyanyl radical adduct. The enzymatic conversion of cyanide to cyanyl radical by peroxidases should be considered in addition to its well-known role as a metal ligand. Furthermore, since cyanide is used routinely as an inhibitor of peroxidases, some consideration should be given to the biochemical consequences of this formation of the cyanyl radical by the catalytic activity of these enzymes.
Moreno
S N
SN
Laboratory of Molecular Biophysics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709.
Stolze
K
K
Janzen
E G
EG
Mason
R P
RP
D003486:Cyanides; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D006861:Hydrogen Peroxide; D008706:Methemoglobin; D010084:Oxidation-Reduction; D010544:Peroxidases; D011190:Potassium Cyanide; D012966:Sodium Cyanide
D003486:Cyanides; D005609:Free Radicals; D008706:Methemoglobin; D006861:Hydrogen Peroxide; D010544:Peroxidases; D011190:Potassium Cyanide; D012966:Sodium Cyanide