Winterbourn C C, Sutton H C
Arch Biochem Biophys. 1984 Nov 15;235(1):116-26. doi: 10.1016/0003-9861(84)90260-1.
The ability of paraquat radicals (PQ+.) generated by xanthine oxidase and glutathione reductase to give H2O2-dependent hydroxyl radical production was investigated. Under anaerobic conditions, paraquat radicals from each source caused chain oxidation of formate to CO2, and oxidation of deoxyribose to thiobarbituric acid-reactive products that was inhibited by hydroxyl radical scavengers. This is in accordance with the following mechanism derived for radicals generated by gamma-irradiation [H. C. Sutton and C. C. Winterbourn (1984) Arch. Biochem. Biophys. 235, 106-115] PQ+. + Fe3+ (chelate)----Fe2+ (chelate) + PQ++ H2O2 + Fe2+ (chelate)----Fe3+ (chelate) + OH- + OH.. Iron-(EDTA) and iron-(diethylenetriaminepentaacetic acid) (DTPA) were good catalysts of the reaction; iron complexed with desferrioxamine or transferrin was not. Extremely low concentrations of iron (0.03 microM) gave near-maximum yields of hydroxyl radicals. In the absence of added chelator, no formate oxidation occurred. Paraquat radicals generated from xanthine oxidase (but not by the other methods) caused H2O2-dependent deoxyribose oxidation. However, inhibition by scavengers was much less than expected for a reaction of hydroxyl radicals, and this deoxyribose oxidation with xanthine oxidase does not appear to be mediated by free hydroxyl radicals. With O2 present, no hydroxyl radical production from H2O2 and paraquat radicals generated by radiation was detected. However, with paraquat radicals continuously generated by either enzyme, oxidation of both formate and deoxyribose was measured. Product yields decreased with increasing O2 concentration and increased with increasing iron(DTPA). These results imply a major difference in reactivity between free and enzymatically generated paraquat radicals, and suggest that the latter could react as an enzyme-paraquat radical complex, for which the relative rate of reaction with Fe3+ (chelate) compared with O2 is greater than is the case with free paraquat radicals.
研究了由黄嘌呤氧化酶和谷胱甘肽还原酶产生的百草枯自由基(PQ+·)产生依赖过氧化氢的羟基自由基的能力。在厌氧条件下,来自每种来源的百草枯自由基导致甲酸链氧化为二氧化碳,以及脱氧核糖氧化为硫代巴比妥酸反应产物,该反应被羟基自由基清除剂抑制。这与γ辐射产生的自由基的以下机制一致[H.C.萨顿和C.C.温特伯恩(1984年)《生物化学与生物物理学报》235卷,106 - 115页]:PQ+· + Fe3+(螯合物)→Fe2+(螯合物) + PQ++;H2O2 + Fe2+(螯合物)→Fe3+(螯合物) + OH- + OH·。铁 - 乙二胺四乙酸(EDTA)和铁 - 二乙烯三胺五乙酸(DTPA)是该反应的良好催化剂;与去铁胺或转铁蛋白络合的铁则不是。极低浓度的铁(0.03微摩尔)产生接近最大产率的羟基自由基。在没有添加螯合剂的情况下,没有发生甲酸氧化。由黄嘌呤氧化酶产生的百草枯自由基(但不是通过其他方法产生的)导致依赖过氧化氢的脱氧核糖氧化。然而,清除剂的抑制作用远低于羟基自由基反应的预期,并且这种由黄嘌呤氧化酶引起的脱氧核糖氧化似乎不是由游离羟基自由基介导的。在有氧气存在的情况下,未检测到由辐射产生的过氧化氢和百草枯自由基产生的羟基自由基。然而,当由任何一种酶持续产生百草枯自由基时,测量到甲酸和脱氧核糖的氧化。产物产率随着氧气浓度的增加而降低,随着铁(DTPA)浓度的增加而增加。这些结果意味着游离和酶促产生的百草枯自由基在反应性上存在重大差异,并表明后者可能作为酶 - 百草枯自由基复合物反应,与Fe3+(螯合物)相比,其与氧气反应的相对速率大于游离百草枯自由基的情况。