文章基本信息

标题：Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. Structure and Properties of Bis[o-xylyldithiolato-μ2-sulfidoferrate(III)], an Analog of the 2Fe-2S Proteins
本地全文：下载
作者：J. J. Mayerle ; R. B. Frankel ; R. H. Holm 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：8
页码：2429-2433
DOI：10.1073/pnas.70.8.2429
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The synthetic analog approach has been applied to a clarification of the active sites of 2Fe-2S* proteins. The compound (Et4N)2[FeS(SCH2)2C6H4]2, derived from o-xylyl-[α],[α]'-dithiol, has been prepared and its structure has been determined by x-ray diffraction. The centrosymmetric anion contains two tetrahedrally coordinated ferric ions bridged by two sulfide ions and separated by 2.70 A. Comparison of electronic, Mossbauer, and proton magnetic resonance spectra and magnetic susceptibility of the anion with the corresponding properties of the oxidized forms of the proteins reveals significant degrees of similarity. The anion also exhibits the essential redox capacity of the proteins. We conclude that [FeS(SCH2)2C6H4]22- possesses the same total oxidation level and electronic configuration as the active sites of the oxidized proteins, and that its structure provides a feasible representation of the minimal structure of the active site. [FeS(SCH2)2C6H4]22- is thus the first well-defined synthetic analog of the active sites of two-iron ferredoxins.
关键词：Fe₂S₂ core ; iron-sulfur complexes ; x-ray diffraction