Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox

Dey A, Glaser T, Couture MMJ, Eltis LD, Holm RH, Hedman B, Hodgson KO, Solomon EI (2004)
Journal of the American Chemical Society 126(26): 8320-8328.

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Abstract
Sulfur K-edge X-ray absorption spectroscopy (XAS) is reported for [Fe4S4](1+,2+,3+) clusters. The results are quantitatively and qualitatively compared with DFT calculations. The change in covalency upon redox in both the [Fe4S4](1+/2+) (ferredoxin) and the [Fe4S4](2+/3+) (HPIP) couple are much larger than that expected from just the change in number of 3d holes. Moreover, the change in the HiPIP couple is higher than that of the ferredoxin couple. These changes in electronic structure are analyzed using DFT calculations in terms of contributions from the nature of the redox active molecular orbital (RAMO) and electronic relaxation. The results indicate that the RAMO of HiPIP has 50% ligand character, and hence, the HiPIP redox couple involves limited electronic relaxation. Alternatively, the RAMO of the ferredoxin couple is metal-based, and the ferredoxin redox couple involves extensive electronic relaxation. The contributions of these RAMO differences to ET processes in the different proteins are discussed.
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Dey A, Glaser T, Couture MMJ, et al. Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox. Journal of the American Chemical Society. 2004;126(26):8320-8328.
Dey, A., Glaser, T., Couture, M. M. J., Eltis, L. D., Holm, R. H., Hedman, B., Hodgson, K. O., et al. (2004). Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox. Journal of the American Chemical Society, 126(26), 8320-8328.
Dey, A., Glaser, T., Couture, M. M. J., Eltis, L. D., Holm, R. H., Hedman, B., Hodgson, K. O., and Solomon, E. I. (2004). Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox. Journal of the American Chemical Society 126, 8320-8328.
Dey, A., et al., 2004. Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox. Journal of the American Chemical Society, 126(26), p 8320-8328.
A. Dey, et al., “Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox”, Journal of the American Chemical Society, vol. 126, 2004, pp. 8320-8328.
Dey, A., Glaser, T., Couture, M.M.J., Eltis, L.D., Holm, R.H., Hedman, B., Hodgson, K.O., Solomon, E.I.: Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox. Journal of the American Chemical Society. 126, 8320-8328 (2004).
Dey, A, Glaser, Thorsten, Couture, MMJ, Eltis, LD, Holm, RH, Hedman, B, Hodgson, KO, and Solomon, EI. “Ligand K-Edge X-ray absorption spectroscopy of [Fe4S4](1+,2+,3+) clusters: Changes in bonding and electronic relaxation upon redox”. Journal of the American Chemical Society 126.26 (2004): 8320-8328.
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Combined Mossbauer spectroscopic, multi-edge X-ray absorption spectroscopic, and density functional theoretical study of the radical SAM enzyme spore photoproduct lyase.
Silver SC, Gardenghi DJ, Naik SG, Shepard EM, Huynh BH, Szilagyi RK, Broderick JB., J. Biol. Inorg. Chem. 19(3), 2014
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Spin-state-dependent oxygen sensitivity of iron dithiolates: sulfur oxygenation or disulfide formation.
O'Toole MG, Kreso M, Kozlowski PM, Mashuta MS, Grapperhaus CA., J. Biol. Inorg. Chem. 13(8), 2008
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Mixed valent sites in biological electron transfer.
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On the accuracy of density functional theory for iron-sulfur clusters.
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Sulfur K-edge X-ray absorption spectroscopy as an experimental probe for S-nitroso proteins.
Szilagyi RK, Schwab DE., Biochem. Biophys. Res. Commun. 330(1), 2005
PMID: 15781232

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