Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment

Dey A, Glaser T, Moura JJG, Holm RH, Hedman B, Hodgson KO, Solomon EI (2004)
Journal of the American Chemical Society 126(51): 16868-16878.

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Ligand K-edge XAS of an [Fe3S4](0) model complex is reported. The pre-edge can be resolved into contributions from the mu(2)S(sulfide), mu(3)S(Sulfide), and S-thiolate ligands. The average ligand-metal bond covalencies obtained from these pre-edges are further distributed between Fe3+ and Fe2.5+ components using DFT calculations. The bridging ligand covalency in the [Fe2S2](+) subsite of the [Fe3S4](0) cluster is found to be significantly lower than its value in a reduced (Fe2S2] cluster (38% vs 61%, respectively). This lowered bridging ligand covalency reduces the superexchange coupling parameter J relative to its value in a reduced [Fe2S2](+) site (-146 cm(-1) vs -360 cm(-1), respectively). This decrease in J, along with estimates of the double exchange parameter Band vibronic coupling parameter lambda(2)/k-, leads to an S = 2 delocalized ground state in the [Fe3S4](0) cluster. The S K-edge XAS of the protein ferredoxin 11 (Fd 11) from the D. gigas active site shows a decrease in covalency compared to the model complex, in the same oxidation state, which correlates with the number of H-bonding interactions to specific sulfur ligands present in the active site. The changes in ligand-metal bond covalencies upon redox compared with DFT calculations indicate that the redox reaction involves a two-electron change (one-electron ionization plus a spin change of a second electron) with significant electronic relaxation. The presence of the redox inactive Fe3+ center is found to decrease the barrier of the redox process in the [Fe3S4] cluster due to its strong antiferromagnetic coupling with the redox active Fe2S2 subsite.
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Dey A, Glaser T, Moura JJG, et al. Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment. Journal of the American Chemical Society. 2004;126(51):16868-16878.
Dey, A., Glaser, T., Moura, J. J. G., Holm, R. H., Hedman, B., Hodgson, K. O., & Solomon, E. I. (2004). Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment. Journal of the American Chemical Society, 126(51), 16868-16878. doi:10.1021/ja0466208
Dey, A., Glaser, T., Moura, J. J. G., Holm, R. H., Hedman, B., Hodgson, K. O., and Solomon, E. I. (2004). Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment. Journal of the American Chemical Society 126, 16868-16878.
Dey, A., et al., 2004. Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment. Journal of the American Chemical Society, 126(51), p 16868-16878.
A. Dey, et al., “Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment”, Journal of the American Chemical Society, vol. 126, 2004, pp. 16868-16878.
Dey, A., Glaser, T., Moura, J.J.G., Holm, R.H., Hedman, B., Hodgson, K.O., Solomon, E.I.: Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment. Journal of the American Chemical Society. 126, 16868-16878 (2004).
Dey, A, Glaser, Thorsten, Moura, JJG, Holm, RH, Hedman, B, Hodgson, KO, and Solomon, EI. “Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4](0,+) clusters: Delocalization, redox, and effect of the protein environment”. Journal of the American Chemical Society 126.51 (2004): 16868-16878.
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