Biochemical requirements for singlet oxygen production by purified human myeloperoxidase.
作者： J R Kanofsky , J Wright , G E Miles-Richardson , A I Tauber
DOI: 10.1172/JCI111562
关键词: Chloride peroxidase 、 Peroxide 、 Singlet oxygen 、 Azide 、 Chemistry 、 Chemiluminescence 、 Inorganic chemistry 、 Yield (chemistry) 、 Oxygen 、 Myeloperoxidase
摘要: The myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-halide systems were found to produce chemiluminescence at 1,268 nm, a characteristic emission band for singlet oxygen (1O2). was enhanced by factor of 29 +/- 5 in deuterium oxide and inhibited the 1O2 quenchers, histidine azide ion. Inactivation MPO with heat or cyanide ion prevented light production. combined weight all data strongly supported production these enzyme systems. amount produced sensitive conditions employed. Under optimal pH 5, MPO-H2O2-bromide (Br-) system 0.42 0.03 mol 1O2/mol H2O2 consumed, close theoretical value 0.5 that predicted reaction stoichiometry. In contrast, MPO-H2O2-chloride (Cl-) much less efficient. maximum yield 0.09 0.02 mol/mol consumed required 4 mM H2O2. At higher pH, rapidly decreased. 7 0.0004 0.0002 consumed. Enzyme inactivation major limiting both Cl- Br-. While MPO-H2O2-halide can efficiently 1O2, are not physiologic, which suggests stimulated neutrophil does derive from generated mechanism.
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