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. 1972 Sep;69(9):2437–2441. doi: 10.1073/pnas.69.9.2437

Structure and Properties of a Synthetic Analogue of Bacterial Iron-Sulfur Proteins

T Herskovitz *, B A Averill *, R H Holm *,†, James A Ibers ‡, W D Phillips §, J F Weiher §
PMCID: PMC426959  PMID: 4506765

Abstract

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, Mössbauer, 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.

Keywords: Fe4S4 core, PMR-iron-sulfur complexes, x-ray diffraction

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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