Mössbauer Spectroscopic Studies of Purified Human Neuromelanin Isolated from the Substantia Nigra

M. Gerlach, A. X. Trautwein, L. Zecca, M. B.H. Youdim, P. Riederer*

*Corresponding author for this work
96 Citations (Scopus)

Abstract

Abstract: 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.

Original languageEnglish
JournalJournal of Neurochemistry
Volume65
Issue number2
Pages (from-to)923-926
Number of pages4
ISSN0022-3042
DOIs
Publication statusPublished - 01.08.1995

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