Xanthine oxidase- and iron-dependent lipid peroxidation.

Xanthine oxidase- and iron-dependent lipid peroxidation.
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DOI:
10.1006/abbi.1993.1107
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发表时间:
1993-02
影响因子:
3.9
通讯作者:
D. Miller;T. Grover;N. Nayini;S. Aust
D. Miller;T. Grover;N. Nayini;S. Aust
中科院分区:
生物学3区
文献类型:
--
作者:
D. Miller;T. Grover;N. Nayini;S. Aust

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黄嘌呤氧化酶和铁依赖性脂质过氧化已被广泛研究,在许多模型系统,但这个过程的一些细节仍然不清楚。由于铁的氧化还原反应是铁催化的脂质过氧化反应的重要参数,我们研究了黄嘌呤氧化酶产生的超氧化物和过氧化氢的作用,氧化和还原铁,从而影响铁催化的脂质过氧化反应。因此,我们比较了黄嘌呤氧化酶和ADP:Fe(III)催化的脂质过氧化反应,黄嘌呤氧化酶和ADP:Fe(II)催化的。超氧阴离子对铁氧化还原作用的研究表明,超氧阴离子是ADP:Fe(II)的较好氧化剂,而不是ADP:Fe(III)的还原剂。超氧化物生成系统(由黄嘌呤氧化酶和过氧化氢酶组成)和ADP:Fe(II)也导致了更大量的脂质过氧化比超氧化物和ADP:Fe(III)。正如预期的那样,过氧化氢仅用作Fe(II)氧化剂。无论是超氧化物或过氧化氢对ADP:Fe(II)和相应的脂质过氧化作用的氧化活性的比较表明,这两种氧化剂大致相当。我们的结论是,超氧化物和过氧化氢,黄嘌呤氧化酶,支持铁催化的脂质过氧化反应,通过参与铁的氧化还原反应,也就是说,他们促进铁(II)氧化或铁(III)还原脂质过氧化反应所必需的。O2-反应的相关性。和H_2O_2对铁的生理螯合物的影响。
Xanthine oxidase and iron-dependent lipid peroxidation has been studied extensively in many model systems, yet several details of this process remain unclear. Because redox reactions of iron are important parameters of iron-catalyzed lipid peroxidation, we have examined the roles of superoxide and hydrogen peroxide, produced by xanthine oxidase, to oxidize and reduce iron and thereby affect iron-catalyzed lipid peroxidation. Thus, we compared lipid peroxidation catalyzed by xanthine oxidase and ADP:Fe(III) to that catalyzed by xanthine oxidase and ADP:Fe(II). An examination of the action of superoxide on iron oxidation and reduction revealed that superoxide is a better oxidant of ADP:Fe(II) than a reductant of ADP:Fe(III). A superoxide generating system (composed of xanthine oxidase and catalase) and ADP:Fe(II) also resulted in a greater amount of lipid peroxidation than superoxide and ADP:Fe(III). Hydrogen peroxide, as expected, only served as an Fe(II) oxidant. A comparison of the oxidant activities of either superoxide or hydrogen peroxide on ADP:Fe(II) and the corresponding effects on lipid peroxidation revealed that both oxidants were roughly equivalent. We conclude that superoxide and hydrogen peroxide, produced from xanthine oxidase, support iron-catalyzed lipid peroxidation through their participation in redox reactions of iron, that is, they facilitate Fe(II) oxidation or Fe(III) reduction necessary for lipid peroxidation. The relevance of the reactions of O2-. and H2O2 on physiological chelates of iron are discussed.