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Structure and Properties of a Synthetic Analogue of Bacterial Iron-Sulfur Proteins
Open accessAbstract
The compound (Et 4 N) 2 [Fe 4 S 4 (SCH 2 Ph) 4 ] has been prepared and its structure determined by x-ray diffraction. The Fe 4 S 4 core of the anion possesses a configuration of D 2d symmetry that is closely related to the Fe 4 S 4 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 [Fe 4 S 4 (SCH 2 Ph) 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 [Fe 4 S 4 (SCH 2 Ph) 4 ] 2- reveal it to be the first well-defined synthetic analogue of the active site of an iron-sulfur protein.
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Cited by
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Metadata
- Authors
- Herskovitz, T., Averill, B. A., Holm, R. H., Ibers, J. A., Phillips, W. D., & Weiher, J. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1972-09
- Volume
- 69
- Issue
- 9
- Pages
- 2437-2441
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2003456382
- Cited by
- 212
- References
- 0
- FWCI
- 21.36
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Herskovitz, T., Averill, B. A., Holm, R. H., Ibers, J. A., Phillips, W. D., & Weiher, J. F. (1972). Structure and Properties of a Synthetic Analogue of Bacterial Iron-Sulfur Proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.69.9.2437
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