Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]
B. A. Averil, T. Herskovitz, R. H. Holm*, James A Ibers
Reaction of ferric chloride in methanol with 3 equiv of sodium mercaptide followed by 1 equiv of a methanolic solution of sodium hydrosulfide and sodium methoxide affords the complexes [Fe4S4(SR)J2~ (R = alkyl, aryl), which may be precipitated and purified in the form of salts of quaternary cations. The crystal structure of a prototype member of the series, [Et4N]2[Fe4S4(SCH2Ph)4], has been determined from 4084 independent reflections collected by counter methods. The red-black crystals are monoclinic, space group C2h-P22lc, with a = 11.922 (6), b = 34.523 (17), and c = 12.762 (5) Á and ß = 95.78 (2)°. The measured density of 1.43 (3) g cm-3 agrees with the density of 1.40 g cm-3, calculated for eight anions and four cations in the cell. The absorption corrected data gave a conventional R factor (on F) of 0.036 on least-squares refinement. The structure consists of discrete anions and cations; the geometry of the tetraethylammonium ion is unexceptional. The core (Fe4S4∗) of the anion exhibits distortions from cubic symmetry which are those of the point group D2c-42m such that each face of the polyhedron is a nonplanar rhomb. The bonded Fe-S∗ distances occur as sets of four (2.239 (4) A) and eight (2.310 (3) Á), giving an average of 2.286 Á. The Fe-Fe distances occur as four short (2.732 (3) A) and two slightly longer (2.776 Á) separations and imply some direct metal-metal interactions. All four iron atoms are structurally indistinguishable. Comparisons of certain structural parameters of [Fe4S4(SCH2Ph)4p with those of the active sites of the reduced high-potential iron protein from Chromatium and the oxidized fer-redoxin from P. aerogenes show that the three structures are unmistakably closely similar. This information together with comparative spectroscopic and magnetic evidence presented elsewhere demonstrates that the synthetic complexes [Fe4S4(SR)4]2- are true analogs of the active sites of bacterial iron-sulfur proteins.
https://doi.org/10.1021/ja00792a013
10.1021/ja00792a013
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Iron-Sulfur Proteins Chemical Compounds
Negative ions Engineering & Materials Science
Positive ions Engineering & Materials Science
Anions Chemical Compounds
Sodium Engineering & Materials Science
Cations Chemical Compounds
Sulfur Engineering & Materials Science
Averil, B. A., Herskovitz, T., Holm, R. H., & Ibers, J. A. (1973). Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]. Journal of the American Chemical Society, 95(11), 3523-3534. https://doi.org/10.1021/ja00792a013
Averil, B. A. ; Herskovitz, T. ; Holm, R. H. ; Ibers, James A. / Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]. In: Journal of the American Chemical Society. 1973 ; Vol. 95, No. 11. pp. 3523-3534.
@article{2b856069cdac4d1da9419bca62eb9871,
title = "Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]",
abstract = "Reaction of ferric chloride in methanol with 3 equiv of sodium mercaptide followed by 1 equiv of a methanolic solution of sodium hydrosulfide and sodium methoxide affords the complexes [Fe4S4(SR)J2~ (R = alkyl, aryl), which may be precipitated and purified in the form of salts of quaternary cations. The crystal structure of a prototype member of the series, [Et4N]2[Fe4S4(SCH2Ph)4], has been determined from 4084 independent reflections collected by counter methods. The red-black crystals are monoclinic, space group C2h-P22lc, with a = 11.922 (6), b = 34.523 (17), and c = 12.762 (5) {\'A} and {\ss} = 95.78 (2)°. The measured density of 1.43 (3) g cm-3 agrees with the density of 1.40 g cm-3, calculated for eight anions and four cations in the cell. The absorption corrected data gave a conventional R factor (on F) of 0.036 on least-squares refinement. The structure consists of discrete anions and cations; the geometry of the tetraethylammonium ion is unexceptional. The core (Fe4S4∗) of the anion exhibits distortions from cubic symmetry which are those of the point group D2c-42m such that each face of the polyhedron is a nonplanar rhomb. The bonded Fe-S∗ distances occur as sets of four (2.239 (4) A) and eight (2.310 (3) {\'A}), giving an average of 2.286 {\'A}. The Fe-Fe distances occur as four short (2.732 (3) A) and two slightly longer (2.776 {\'A}) separations and imply some direct metal-metal interactions. All four iron atoms are structurally indistinguishable. Comparisons of certain structural parameters of [Fe4S4(SCH2Ph)4p with those of the active sites of the reduced high-potential iron protein from Chromatium and the oxidized fer-redoxin from P. aerogenes show that the three structures are unmistakably closely similar. This information together with comparative spectroscopic and magnetic evidence presented elsewhere demonstrates that the synthetic complexes [Fe4S4(SR)4]2- are true analogs of the active sites of bacterial iron-sulfur proteins.",
author = "Averil, {B. A.} and T. Herskovitz and Holm, {R. H.} and Ibers, {James A}",
doi = "10.1021/ja00792a013",
Averil, BA, Herskovitz, T, Holm, RH & Ibers, JA 1973, 'Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]', Journal of the American Chemical Society, vol. 95, no. 11, pp. 3523-3534. https://doi.org/10.1021/ja00792a013
Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]. / Averil, B. A.; Herskovitz, T.; Holm, R. H.; Ibers, James A.
In: Journal of the American Chemical Society, Vol. 95, No. 11, 01.05.1973, p. 3523-3534.
T1 - Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]
AU - Averil, B. A.
AU - Herskovitz, T.
AU - Holm, R. H.
AU - Ibers, James A
N2 - Reaction of ferric chloride in methanol with 3 equiv of sodium mercaptide followed by 1 equiv of a methanolic solution of sodium hydrosulfide and sodium methoxide affords the complexes [Fe4S4(SR)J2~ (R = alkyl, aryl), which may be precipitated and purified in the form of salts of quaternary cations. The crystal structure of a prototype member of the series, [Et4N]2[Fe4S4(SCH2Ph)4], has been determined from 4084 independent reflections collected by counter methods. The red-black crystals are monoclinic, space group C2h-P22lc, with a = 11.922 (6), b = 34.523 (17), and c = 12.762 (5) Á and ß = 95.78 (2)°. The measured density of 1.43 (3) g cm-3 agrees with the density of 1.40 g cm-3, calculated for eight anions and four cations in the cell. The absorption corrected data gave a conventional R factor (on F) of 0.036 on least-squares refinement. The structure consists of discrete anions and cations; the geometry of the tetraethylammonium ion is unexceptional. The core (Fe4S4∗) of the anion exhibits distortions from cubic symmetry which are those of the point group D2c-42m such that each face of the polyhedron is a nonplanar rhomb. The bonded Fe-S∗ distances occur as sets of four (2.239 (4) A) and eight (2.310 (3) Á), giving an average of 2.286 Á. The Fe-Fe distances occur as four short (2.732 (3) A) and two slightly longer (2.776 Á) separations and imply some direct metal-metal interactions. All four iron atoms are structurally indistinguishable. Comparisons of certain structural parameters of [Fe4S4(SCH2Ph)4p with those of the active sites of the reduced high-potential iron protein from Chromatium and the oxidized fer-redoxin from P. aerogenes show that the three structures are unmistakably closely similar. This information together with comparative spectroscopic and magnetic evidence presented elsewhere demonstrates that the synthetic complexes [Fe4S4(SR)4]2- are true analogs of the active sites of bacterial iron-sulfur proteins.
AB - Reaction of ferric chloride in methanol with 3 equiv of sodium mercaptide followed by 1 equiv of a methanolic solution of sodium hydrosulfide and sodium methoxide affords the complexes [Fe4S4(SR)J2~ (R = alkyl, aryl), which may be precipitated and purified in the form of salts of quaternary cations. The crystal structure of a prototype member of the series, [Et4N]2[Fe4S4(SCH2Ph)4], has been determined from 4084 independent reflections collected by counter methods. The red-black crystals are monoclinic, space group C2h-P22lc, with a = 11.922 (6), b = 34.523 (17), and c = 12.762 (5) Á and ß = 95.78 (2)°. The measured density of 1.43 (3) g cm-3 agrees with the density of 1.40 g cm-3, calculated for eight anions and four cations in the cell. The absorption corrected data gave a conventional R factor (on F) of 0.036 on least-squares refinement. The structure consists of discrete anions and cations; the geometry of the tetraethylammonium ion is unexceptional. The core (Fe4S4∗) of the anion exhibits distortions from cubic symmetry which are those of the point group D2c-42m such that each face of the polyhedron is a nonplanar rhomb. The bonded Fe-S∗ distances occur as sets of four (2.239 (4) A) and eight (2.310 (3) Á), giving an average of 2.286 Á. The Fe-Fe distances occur as four short (2.732 (3) A) and two slightly longer (2.776 Á) separations and imply some direct metal-metal interactions. All four iron atoms are structurally indistinguishable. Comparisons of certain structural parameters of [Fe4S4(SCH2Ph)4p with those of the active sites of the reduced high-potential iron protein from Chromatium and the oxidized fer-redoxin from P. aerogenes show that the three structures are unmistakably closely similar. This information together with comparative spectroscopic and magnetic evidence presented elsewhere demonstrates that the synthetic complexes [Fe4S4(SR)4]2- are true analogs of the active sites of bacterial iron-sulfur proteins.
U2 - 10.1021/ja00792a013
DO - 10.1021/ja00792a013
Averil BA, Herskovitz T, Holm RH, Ibers JA. Synthetic Analogs of the Active Sites of Iron-Sulfur Proteins. II.1 Synthesis and Structure of the Tetra[mercapto-m3-sulfndo-iron] Clusters, [Fe4s4(SR)4]. Journal of the American Chemical Society. 1973 May 1;95(11):3523-3534. https://doi.org/10.1021/ja00792a013