Faculdade de Ciências e Tecnologia (FCT) >
FCT Departamentos >
FCT: Departamento de Química >
FCT: DQ - Artigos em revista internacional com arbitragem científica >
Please use this identifier to cite or link to this item:
|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|
Moura, José J. G.
|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|
|Publisher version: ||http://pubs.acs.org/doi/pdfplus/10.1021/ja0466208|
|Appears in Collections:||FCT: DQ - Artigos em revista internacional com arbitragem científica|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.