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标题：Structure and Properties of a Synthetic Analogue of Bacterial Iron-Sulfur Proteins
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作者：T. Herskovitz ; B. A. Averill ; 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：1972
卷号：69
期号：9
页码：2437-2441
DOI：10.1073/pnas.69.9.2437
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The compound (Et4N)2[Fe4S4(SCH2Ph)4] has been prepared and its structure determined by x-ray diffraction. The Fe4S4 core of the anion possesses a configuration of D2d symmetry that is closely related to the Fe4S4 active-site structures of the high-potential iron protein from Chromatium and the ferredoxin from Micrococcus aerogenes. Electronic properties of the tetrameric anion have been partially characterized by measurement of proton magnetic resonance, Mossbauer, photoelectron, and electronic spectra, and magnetic susceptibility. Comparison of corresponding properties of [Fe4S4(SCH2Ph)4]2- and the proteins implies that the oxidation levels of the synthetic tetramer, the reduced form of the high-potential protein, and the oxidized form of the 8-Fe ferredoxins are equivalent. The tetramer possesses the one-electron redox capacity associated with the 4-Fe centers of the ferredoxins. The structural and collective electronic features of [Fe4S4(SCH2Ph)4]2- reveal it to be the first well-defined synthetic analogue of the active site of an iron-sulfur protein.
关键词：Fe₄S₄ core ; PMR-iron-sulfur complexes ; x-ray diffraction