Structure and properties of a synthetic analogue o...[Proc Natl Acad Sci U S A. 1972]

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1: Proc Natl Acad Sci U S A. 1972 Sep;69(9):2437-41. Links

Structure and properties of a synthetic analogue of bacterial iron--sulfur proteins.

Herskovitz T, Averill BA, Holm RH, Ibers JA, Phillips WD, Weiher JF.

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.

PMID: 4506765 [PubMed - indexed for MEDLINE]

PMCID: PMC426959

Synthetic analogs of the active sites of iron-sulfur proteins. Structure and properties of bis(o-xylyldithiolato-m2-sulfidoferrate (3)), an analog of the 2Fe-2S proteins.
Proc Natl Acad Sci U S A. 1973 Aug; 70(8):2429-33.

[Proc Natl Acad Sci U S A. 1973]
Synthetic analogs of active sites of iron-sulfur proteins: bis (o-xylyldithiolato) ferrate (III) monoanion, a structurally unconstrained model for the rubredoxin Fe-S4 unit.
Proc Natl Acad Sci U S A. 1975 Aug; 72(8):2868-72.

[Proc Natl Acad Sci U S A. 1975]
High-nuclearity sulfide-rich molybdenum[bond]iron[bond]sulfur clusters: reevaluation and extension.
Inorg Chem. 2002 Jun 17; 41(12):3191-201.

[Inorg Chem. 2002]
ReviewIron-sulfur proteins: structural chemistry of their chromophores and related systems.
Angew Chem Int Ed Engl. 1973 May; 12(5):390-9.

[Angew Chem Int Ed Engl. 1973]
ReviewNMR spectroscopic studies of paramagnetic proteins: iron-sulfur proteins.
Annu Rev Biophys Biomol Struct. 1995; 24:209-37.

[Annu Rev Biophys Biomol Struct. 1995]
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Cited by 11 PubMed Central articles

The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters.
Bruice TC, Maskiewicz R, Job R. Proc Natl Acad Sci U S A. 1975 Jan; 72(1):231-234.

[Proc Natl Acad Sci U S A. 1975]
A role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations.
Sligar SG, Debrunner PG, Lipscomb JD, Namtvedt MJ, Gunsalus IC. Proc Natl Acad Sci U S A. 1974 Oct; 71(10):3906-10.

[Proc Natl Acad Sci U S A. 1974]
Synthetic analogs of the active sites of iron-sulfur proteins. Structure and properties of bis(o-xylyldithiolato-m2-sulfidoferrate (3)), an analog of the 2Fe-2S proteins.
Mayerle JJ, Frankel RB, Holm RH, Ibers JA, Phillips WD, Weiher JF. Proc Natl Acad Sci U S A. 1973 Aug; 70(8):2429-33.

[Proc Natl Acad Sci U S A. 1973]
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Cited by 11 PubMed Central articles

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