黄嘌呤氧化酶介导铁蛋白释放铁。超氧自由基的作用。
Release of iron from ferritin by xanthine oxidase. Role of the superoxide radical.
作者信息
Bolann B J, Ulvik R J
出版信息
Biochem J. 1987 Apr 1;243(1):55-9. doi: 10.1042/bj2430055.
Abstract
Mobilization of iron from ferritin by xanthine oxidase was studied under aerobic and anaerobic conditions. Aerobic iron release amounted to approx. 3.7 nmol/ml in 10 min. This amount was decreased by approx. 30% under anaerobic conditions. Aerobic iron mobilization involved two mechanisms. About 70% was released by O2.- generated by xanthine oxidase. The rest was released by O2(.-)-independent mechanisms, which also accounted for the total iron release when O2 was absent. A possible transfer of reducing equivalents directly from xanthine oxidase to ferritin is discussed. The results imply that, in pathological conditions with increased formation of O2.-, iron may be released from ferritin. Furthermore, in hypoxic tissues xanthine oxidase can release iron from ferritin by an O2(.-)-independent process. Free iron is liable to catalyse the formation of the extremely reactive and damaging OH. radical.
摘要
在有氧和无氧条件下，研究了黄嘌呤氧化酶从铁蛋白中动员铁的情况。有氧条件下，铁释放量在10分钟内约为3.7 nmol/ml。在无氧条件下，这一释放量减少了约30%。有氧铁动员涉及两种机制。约70%的铁由黄嘌呤氧化酶产生的超氧阴离子（O₂⁻）释放。其余的铁则通过不依赖超氧阴离子（O₂⁻）的机制释放，在无氧时这种机制也导致了铁的全部释放。文中讨论了还原当量可能直接从黄嘌呤氧化酶转移到铁蛋白的情况。结果表明，在超氧阴离子（O₂⁻）生成增加的病理条件下，铁可能从铁蛋白中释放出来。此外，在缺氧组织中，黄嘌呤氧化酶可通过不依赖超氧阴离子（O₂⁻）的过程从铁蛋白中释放铁。游离铁易于催化形成极具反应性和破坏性的羟基自由基（·OH）。
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