Interaction of peroxynitrite and hydrogen peroxide with dinitrosyl iron complexes containing thiol ligands in vitro.
The interaction of peroxynitrite with thiolate dinitrosyl iron complexes (DNIC) has been examined and compared with the interaction with H2O2. Peroxynitrite oxidized DNIC containing various thiolate ligands--cysteine, glutathione, and bovine serum albumin. Analysis of the oxidation suggested a two-electron reaction and gave third-order rate constants of (9.3 +/- 0.5).109 M-2.sec-1 for DNIC with BSA, (4.0 +/- 0.3).108 M-2.sec-1 for DNIC with cysteine, and (1. 8 +/- 0.3).107 M-2.sec-1 for DNIC with glutathione at 20 degrees C and pH 7.6. Peroxynitrite was more reactive towards DNIC than towards sulfhydryls. Addition of sodium dithionite after the reaction led to significant restoration of the EPR signal of DNIC with cysteine. The reaction of glutathione DNIC with H2O2 was about 600 times slower than with ONOO- and not reversed by sodium dithionite. Thus peroxynitrite, in contrast to hydrogen peroxide, changes the pool of nitrosocompounds which can be responsible for interconversion, storage, and transportation of nitric oxide in vivo.
Lobysheva
I I
II
Institute of Chemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia. irlobysh@polymer.chph.ras.ru irlobysh@polymer.chph.ras.ru
Serezhenkov
V A
VA
Vanin
A F
AF
D003545:Cysteine / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D005978:Glutathione / Q000737:chemistry; D006861:Hydrogen Peroxide / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008024:Ligands; D009566:Nitrates / Q000737:chemistry*; D009603:Nitroso Compounds / Q000737:chemistry*; D010084:Oxidation-Reduction; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D008024:Ligands; D009566:Nitrates; D009603:Nitroso Compounds; D013438:Sulfhydryl Compounds; C039642:peroxynitric acid; D012710:Serum Albumin, Bovine; D006861:Hydrogen Peroxide; D007501:Iron; D005978:Glutathione; D003545:Cysteine