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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/8319

Title: Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4]0,+ clusters: delocalization, redox, and effect of the protein environment
Authors: Dey, A
Glaser, T
Moura, José J. G.
Holm, RH
Hedman, B
Hodgson, KO
Solomon, EI
Issue Date: 2004
Publisher: American Chemical Society
Abstract: Ligand K-edge XAS of an [Fe3S4]0 model complex is reported. The pre-edge can be resolved into contributions from the í2Ssulfide, í3Ssulfide, and Sthiolate 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 B and vibronic coupling parameter ì2/k-, leads to an S ) 2 delocalized ground state in the [Fe3S4]0 cluster. The S K-edge XAS of the protein ferredoxin II (Fd II) 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.
Peer Reviewed: yes
URI: http://hdl.handle.net/10362/8319
Publisher version: http://pubs.acs.org/doi/pdfplus/10.1021/ja0466208
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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