Gerlach M, Trautwein A X, Zecca L, Youdim M B, Riederer P
Department of Clinical Neurochemistry, University Hospital for Psychiatry, Julius-Maximilians-Universität, Würzburg, Germany.
J Neurochem. 1995 Aug;65(2):923-6. doi: 10.1046/j.1471-4159.1995.65020923.x.
57Fe Mössbauer spectroscopy at different temperatures has been used to characterize the nature of purified human neuromelanin isolated from the substantia nigra. The quantitative determination of iron(III) by estimation of the overall area of the Mössbauer spectrum at room temperature reveals an iron content of 2.8 +/- 1.4%. No subspectra corresponding to divalent iron could be observed in these spectra. The derived Mössbauer parameters lead to the conclusion that the iron sites in the human neuromelanin are similar to those of human hemosiderin (or ferritin). However, owing to the water insolubility of the purified neuromelanin, it must be concluded that the neuromelanin hemosiderin (or ferritin) is bound in a protein matrix that makes it insoluble and difficult to stain histochemically. This protein attachment to neuromelanin is important in that it is what makes it different from synthetic dopamine melanin.
利用不同温度下的57Fe穆斯堡尔光谱对从黑质中分离出的纯化人神经黑色素的性质进行了表征。通过估计室温下穆斯堡尔光谱的总面积对铁（III）进行定量测定，结果显示铁含量为2.8±1.4%。在这些光谱中未观察到对应于二价铁的子光谱。推导得到的穆斯堡尔参数得出结论，人神经黑色素中的铁位点与人类血铁黄素（或铁蛋白）的铁位点相似。然而，由于纯化的神经黑色素不溶于水，必须得出结论，神经黑色素血铁黄素（或铁蛋白）结合在一种蛋白质基质中，这使其不溶且难以进行组织化学染色。这种蛋白质与神经黑色素的附着很重要，因为它使神经黑色素不同于合成多巴胺黑色素。
