title: Ligand K-edge X-ray absorption spectroscopy and DFT calculations on [Fe3S4]0,+ clusters: delocalization, redox, and effect of the protein environment.
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 Fe(3+) and Fe(2.5+) 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 lambda2/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 Fe(3+) 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.
authors.affiliation: Department of Chemistry and Stanford Synchrotron Radiation Laboratory, Stanford University, Stanford, CA 94305, USA.
authors.forename: Abhishek
authors.initials: A
authors.lastname: Dey
authors.forename: Thorsten
authors.initials: T
authors.lastname: Glaser
authors.forename: Jose J-G
authors.initials: JJ
authors.lastname: Moura
authors.forename: Richard H
authors.initials: RH
authors.lastname: Holm
authors.forename: Britt
authors.initials: B
authors.lastname: Hedman
authors.forename: Keith O
authors.initials: KO
authors.lastname: Hodgson
authors.forename: Edward I
authors.initials: EI
authors.lastname: Solomon
mesh_terms: D001665:Binding Sites; D005288:Ferredoxins / Q000737:chemistry; D007501:Iron / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D010084:Oxidation-Reduction; D013052:Spectrometry, X-Ray Emission; D013455:Sulfur / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D013455:Sulfur; D007501:Iron