Chlorination of NADH: similarities of the HOCl-supported and chloroperoxidase-catalyzed reactions
作者： Brenda W. Griffin , Robert Haddox
DOI: 10.1016/0003-9861(85)90840-9
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摘要: The chloroperoxidase-catalyzed reactions of NAD(P)H with H2O2 in the presence Cl- or Br- have been characterized. With 1 mol per NADH, one atom 36Cl was incorporated into 264-nm-absorbing intermediate product. This species oxidized enzymatically by a second mole to distinct from NAD+, which retained Cl atom. Spectroscopically identical were also produced reaction NADH and two molar ratios HOCl, respectively. These data indicate that, respect halogenation activities, chloroperoxidase functions similarly myeloperoxidase, i.e., produces HOCl as first product oxidation H2O2. Moreover, rapid chlorination followed may be an important highly lethal microbicidal effect myeloperoxidase activated neutrophils.
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