title: (I,0) Mixed-valence state of a diiron complex with pertinence to the [FeFe]-hydrogenase active site: an IR, EPR, and computational study.
abstract: Biphenyl-2,2'-dithiolate (bpdt) bridged Fe(2)(bpdt)(CO)(6) (1) undergoes two sequential electrochemically quasi-reversible reductions. The one-electron reduction product 1(-) is unusually stable against irreversible structural changes and could be characterized by IR and EPR spectroscopy supported by computational methods. Reduction to the (I,0) state does not trigger bridging coordination of CO but partial deligation of the dithiolate in 1(-) that ultimately forms a diamagnetic dimerization product.
authors.affiliation: Department of Photochemistry and Molecular Science, The Angstrom Laboratories, Uppsala University, BOX 532, 751 20 Uppsala, Sweden.
authors.forename: Pradyumna S
authors.initials: PS
authors.lastname: Singh
authors.forename: Hans Christian
authors.initials: HC
authors.lastname: Rudbeck
authors.forename: Ping
authors.initials: P
authors.lastname: Huang
authors.forename: Salah
authors.initials: S
authors.lastname: Ezzaher
authors.forename: Lars
authors.initials: L
authors.lastname: Eriksson
authors.forename: Matthias
authors.initials: M
authors.lastname: Stein
authors.forename: Sascha
authors.initials: S
authors.lastname: Ott
authors.forename: Reiner
authors.initials: R
authors.lastname: Lomoth
mesh_terms: D020134:Catalytic Domain; D004578:Electron Spin Resonance Spectroscopy; D005290:Ferric Compounds / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D013055:Spectrophotometry, Infrared
chemical_list: D005290:Ferric Compounds; D007506:Iron-Sulfur Proteins; C118830:iron hydrogenase; D006864:Hydrogenase