Oxidation of biological electron donors and antioxidants by a reactive lactoperoxidase metabolite from nitrite (NO2-): an EPR and spin trapping study.
Oxidation of biological electron donors and antioxidants by a reactive lactoperoxidase metabolite from nitrite (NO2-): an EPR and spin trapping study.
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亚硝酸盐 (NO2-) 中的活性乳过氧化物酶代谢物对生物电子供体和抗氧化剂的氧化:一项 EPR 和自旋捕获研究。
DOI:
10.1016/s0891-5849(98)00244-5
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发表时间:
1999
影响因子:
7.4
通讯作者:
Dillon,J
中科院分区:
文献类型:
--
作者:
Reszka,KJ;Matuszak,Z;Chignell,CF;Dillon,J
We report that a lactoperoxidase (LPO) metabolite derived from nitrite (NO2−) catalyses one-electron oxidation of biological electron donors and antioxidants such as NADH, NADPH, cysteine, glutathione, ascorbate, and Trolox C. The radical products of the reaction have been detected and identified using either direct EPR or EPR combined with spin trapping. While LPO/H2O2alone generated only minute amounts of radicals from these compounds, the yield of radicals increased sharply when nitrite was also present. In aerated buffer (pH 7) the nitrite-dependent oxidation of NAD(P)H by LPO/H2O2produced superoxide radical, O2•−, which was detected as a DMPO/O2H adduct. We propose that in the LPO/H2O2/NO2−/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2alone. Because both nitrite and peroxidase enzymes are ubiquitous our observations point at a possible mechanism through which nitrite might exert its biological and cytotoxic action in vivo, and identify some of the physiological targets which might be affected by the peroxidase/H2O2/nitrite systems.