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.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
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.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

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.
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.
This data publication is cited in the following publications:
This publication cites the following data publications:

12 Citations in Europe PMC

Data provided by Europe PubMed Central.

Spectroscopic and redox studies of valence-delocalized [Fe2S2](+) centers in thioredoxin-like ferredoxins.
Subramanian S, Duin EC, Fawcett SE, Armstrong FA, Meyer J, Johnson MK., J. Am. Chem. Soc. 137(13), 2015
PMID: 25790339
S K-edge XAS and DFT calculations on cytochrome P450: covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity.
Dey A, Jiang Y, Ortiz de Montellano P, Hodgson KO, Hedman B, Solomon EI., J. Am. Chem. Soc. 131(22), 2009
PMID: 19438234
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
PMID: 18633652
Mixed valent sites in biological electron transfer.
Solomon EI, Xie X, Dey A., Chem Soc Rev 37(4), 2008
PMID: 18362972
Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on superoxide reductase: role of the axial thiolate in reactivity.
Dey A, Jenney FE Jr, Adams MW, Johnson MK, Hodgson KO, Hedman B, Solomon EI., J. Am. Chem. Soc. 129(41), 2007
PMID: 17887751
How does single oxygen atom addition affect the properties of an Fe-nitrile hydratase analogue? The compensatory role of the unmodified thiolate.
Lugo-Mas P, Dey A, Xu L, Davin SD, Benedict J, Kaminsky W, Hodgson KO, Hedman B, Solomon EI, Kovacs JA., J. Am. Chem. Soc. 128(34), 2006
PMID: 16925440
Sulfur K-edge XAS and DFT calculations on nitrile hydratase: geometric and electronic structure of the non-heme iron active site.
Dey A, Chow M, Taniguchi K, Lugo-Mas P, Davin S, Maeda M, Kovacs JA, Odaka M, Hodgson KO, Hedman B, Solomon EI., J. Am. Chem. Soc. 128(2), 2006
PMID: 16402841

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 15612726
PubMed | Europe PMC

Search this title in

Google Scholar