REDUCTIVE MOBILIZATION OF FERRITIN IRON
REDUCTIVE MOBILIZATION OF FERRITIN IRON
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DOI：
10.1111/j.1432-1033.1985.tb09177.x
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发表时间：
1985-01-01
期刊：
影响因子：
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通讯作者：
SCHNEIDER, W
中科院分区：
文献类型：
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作者：
FUNK, F;LENDERS, JP;SCHNEIDER, W
研究了铁蛋白（铁储存的主要蛋白质）中铁的还原动员。我们发现连二亚硫酸盐、巯基乙酸盐和二氢核黄素-5''-磷酸盐 (FMNH2) 释放铁的动力学特征差异很大。连二亚硫酸盐还原对 pH 值的依赖性最为明显，pH 4 时的还原速度比 pH 7 时快 100 倍。实验数据可以用产物或离析物与铁蛋白核心的界面氢氧化铁 (III) 的特定相互作用来一致地解释。假定在连二亚硫酸盐反应中与产物亚硫酸盐形成表面络合物，并在巯基乙酸酯反应中与离析物形成表面络合物。铁(II) 与自由基阴离子FMN- 的络合物被认为参与了FMNH2 的铁释放。一系列不同尺寸和配位性质的硫醇对铁的动员证实了表面复合物形成的重要性。没有发现证据表明受阻炮弹穿透的主要影响。
The reductive mobilisation of iron from ferritin, the principal protein of iron storage, was studied. The kinetic characteristics of iron release by dithionite, thioglycolate, and dihydroriboflavin-5''-phosphate (FMNH2) were found to differ widely. The dependence on pH is most pronounced for the dithionite reduction which proceeds 100 times faster at pH 4 than at pH 7. The experimental data can be consistently explained in terms of specific interactions of products or educts with interfacial iron(III) hydroxide of the ferritin core. Surface complexes with the product sulfite are postulated in the dithionite reaction, and with the educt in the thioglycollate reaction. Iron(II) complexes with the radical anion FMN- are suggested to be involved in the iron release by FMNH2. The mobilization of iron by a series of thiols of different size and coordinative properties confirmed the importance of surface complex formation. No evidence was found for predominant effects of hindered shell penetration.