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Mossbauer, electron paramagnetic resonance, and theoretical studies of a carbene-based all-ferrous Fe4S4 cluster: electronic origin and structural identification of the unique spectroscopic site.

ABSTRACT: It is well established that the cysteinate-coordinated [Fe(4)S(4)] cluster of the iron protein of nitrogenase from Azotobacter vinelandii (Av2) can attain the all-ferrous core oxidation state. Mössbauer and electron paramagnetic resonance (EPR) studies have shown that the all-ferrous cluster has a ground-state spin S = 4 and an effective 3:1 site symmetry in the spin structure and (57)Fe quadrupole interactions. Recently, Deng and Holm reported the synthesis of [Fe(4)S(4)(Pr(i)(2)NHCMe(2))(4)],(2) (1; Pr(i)(2)NHCMe(2) = 1,3-diisopropyl-4,5-dimethylimidazol-2-ylidene) and showed that the all-ferrous carbene-coordinated cluster is amenable to physicochemical studies. Mössbauer and EPR studies of 1, reported here, reveal that the electronic structure of this complex is strikingly similar to that of the protein-bound cluster, suggesting that the ground-state spin and the 3:1 site ratio are consequences of spontaneous distortions of the cluster core. To gain insight into the origin of the peculiar ground state of the all-ferrous clusters in 1 and Av2, we have studied a theoretical model that is based on a Heisenberg-Dirac-van Vleck Hamiltonian whose exchange-coupling constants are a function of the Fe-Fe distances. By combining the exchange energies with the elastic deformation energies in the harmonic approximation, we obtain for a T(2) distortion a minimum with spin S = 4 and a C(3v) core structure in which one iron is unique and three irons are equivalent. This minimum has all of the spectroscopic and structural characteristics of the all-ferrous clusters of 1 and Av2. Our analysis maps the unique spectroscopic iron site to a specific site in the X-ray structure of the [Fe(4)S(4)](0) core both in complex 1 and in Av2.

SUBMITTER: Chakrabarti M

PROVIDER: S-EPMC2745965 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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Mössbauer, electron paramagnetic resonance, and theoretical studies of a carbene-based all-ferrous Fe4S4 cluster: electronic origin and structural identification of the unique spectroscopic site.

Chakrabarti Mrinmoy M Deng Liang L Holm R H RH Münck Eckard E Bominaar Emile L EL

Inorganic chemistry 20090401 7

It is well established that the cysteinate-coordinated [Fe(4)S(4)] cluster of the iron protein of nitrogenase from Azotobacter vinelandii (Av2) can attain the all-ferrous core oxidation state. Mössbauer and electron paramagnetic resonance (EPR) studies have shown that the all-ferrous cluster has a ground-state spin S = 4 and an effective 3:1 site symmetry in the spin structure and (57)Fe quadrupole interactions. Recently, Deng and Holm reported the synthesis of [Fe(4)S(4)(Pr(i)(2)NHCMe(2))(4)],( ...[more]

PMID: 19326927

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Project description:High-spin Fe(IV)-oxo species are known to be kinetically competent oxidants in non-heme iron enzymes. The properties of these oxidants are not as well understood as the corresponding intermediate-spin oxidants of heme complexes. The present work gives a detailed characterization of the structurally similar complexes [Fe(IV)H(3)buea(O)](-), [Fe(III)H(3)buea(O)](2-), and [Fe(III)H(3)buea(OH)](-) (H(3)buea = tris[(N'-tert-butylureaylato)-N-ethylene]aminato) using Mössbauer and dual-frequency/dual-mode electron paramagnetic resonance (EPR) spectroscopies. The [Fe(IV)H(3)buea(O)](-) complex has a high-spin (S = 2) configuration imposed by the C(3)-symmetric ligand. The EPR spectra of the [Fe(IV)H(3)buea(O)](-) complex presented here represent the first documented examples of an EPR signal from an Fe(IV)-oxo complex, demonstrating the ability to detect and quantify Fe(IV) species with EPR spectroscopy. Quantitative simulations allowed the determination of the zero-field parameter, D = +4.7 cm(-1), and the species concentration. Density functional theory (DFT) calculations of the zero-field parameter were found to be in agreement with the experimental value and indicated that the major contribution to the D value is from spin-orbit coupling of the ground state with an excited S = 1 electronic configuration at 1.2 eV. (17)O isotope enrichment experiments allowed the determination of the hyperfine constants ((17)O)A(z) = 10 MHz for [Fe(IV)H(3)buea(O)](-) and ((17)O)A(y) = 8 MHz, ((17)O)A(z) = 12 MHz for [Fe(III)H(3)buea(OH)](-). The isotropic hyperfine constant (((17)O)A(iso) = -16.8 MHz) was derived from the experimental value to allow a quantitative determination of the spin polarization (?(p) = 0.56) of the oxo p orbitals of the Fe-oxo bond in [Fe(IV)H(3)buea(O)](-). This is the first experimental determination for non-heme complexes and indicates significant covalency in the Fe-oxo bond. High-field Mössbauer spectroscopy gave an (57)Fe A(dip) tensor of (+5.6, +5.3, -10.9) MHz and A(iso) = -25.9 MHz for the [Fe(IV)H(3)buea(O)](-) complex, and the results of DFT calculations were in agreement with the nuclear parameters of the complex.

Dataset Information

Mossbauer, electron paramagnetic resonance, and theoretical studies of a carbene-based all-ferrous Fe4S4 cluster: electronic origin and structural identification of the unique spectroscopic site.

Publications

Mössbauer, electron paramagnetic resonance, and theoretical studies of a carbene-based all-ferrous Fe4S4 cluster: electronic origin and structural identification of the unique spectroscopic site.

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