Chlorination of NADH: similarities of the HOCl-supported and chloroperoxidase-catalyzed reactions.
The chloroperoxidase-catalyzed reactions of NAD(P)H with H2O2 in the presence of Cl- or Br- have been characterized. With 1 mol H2O2 per mol of NADH, one atom of 36Cl was incorporated into the 264-nm-absorbing intermediate product. This species was oxidized enzymatically by a second mole of H2O2 to a species distinct from NAD+, which retained one Cl atom. Spectroscopically identical species were also produced by reaction of NADH with one and two molar ratios of HOCl, respectively. These data indicate that, with respect to halogenation activities, chloroperoxidase functions similarly to myeloperoxidase, i.e., produces HOCl as the first product of Cl- oxidation by H2O2. Moreover, rapid chlorination of NAD(P)H followed by oxidation may be an important and highly lethal microbicidal effect of HOCl produced by myeloperoxidase in activated neutrophils.
Griffin
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Haddox
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D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D002711:Chloride Peroxidase; D002712:Chlorides; D006861:Hydrogen Peroxide; D006863:Hydrogen-Ion Concentration; D009249:NADP; D010084:Oxidation-Reduction; D009195:Peroxidase; D010544:Peroxidases
D002712:Chlorides; D009249:NADP; D006861:Hydrogen Peroxide; D010544:Peroxidases; D002711:Chloride Peroxidase; D009195:Peroxidase