EPR investigations of the iron domain in neuromelanin
EPR investigations of the iron domain in neuromelanin
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DOI：
10.1016/s0925-4439(97)00014-8
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发表时间：
1997-07-10
影响因子：
6.2
通讯作者：
Lopiano, L
中科院分区：
文献类型：
--
作者：
Aime, S;Bergamasco, B;Lopiano, L
本文用电子顺磁共振（EPR）方法研究了铁与神经黑色素（NM）的相互作用。从正常人中脑提取的NM标本的变温EPR光谱特征清楚地表明，铁是作为多核氧-羟基铁聚集体以及孤立的Fe（III）中心。铁氧-羟基相是典型的铁储存蛋白铁蛋白和含铁血黄素，但铁蛋白和NM的变温EPR谱的比较突出了两个铁（III）氧-羟基结构域之间的显着差异。此外，对在铁蛋白或铁盐作为铁源的存在下合成的黑色素模型的进一步研究表明，无论铁的来源是什么，在NM和模型系统中，多核氧化铁的形成和包含的相同途径都在起作用。
The interactions between iron and neuromelanin (NM) have been studied by means of EPR spectroscopy. The variable temperature EPR spectral features of a specimen of NM extracted from normal human midbrains clearly indicate that iron is present as polynuclear oxy-hydroxy ferric aggregates as well as isolated Fe(III) centres. Ferric oxy-hydroxy phases are typical of the iron storage proteins ferritin and hemosiderin, but the comparison of the variable temperature EPR spectra of ferritin and NM highlights significant differences between the two iron(III)oxy-hydroxy domains. Moreover, further investigations on melanin models synthesised in the presence of either ferritin or a ferric salt as iron sources suggest that the same pathway of formation and inclusion of the polynuclear iron oxide is operating in NM and in the model systems, whatever is the source of iron.