title: A super-reduced diferrous [2Fe-2S] cluster.
abstract: A biomimetic [2Fe-2S] cluster has been isolated in the fully reduced diferrous form and characterized by X-ray diffraction. This completes a consistent series of synthetic analogues of protein-bound [2Fe-2S](z) redox centers (z = 2+, 1+, 0) with identical capping ligands. (57)Fe Mössbauer data of the extremely oxidation-sensitive complex compare well with those of the very few reports of all-ferrous ferredoxins and Rieske centers; they confirm the S(T) = 0 ground state and establish a lower limit for the exchange coupling, -J ≥ 30 cm(-1).
authors: Institute of Inorganic Chemistry, Georg-August-University Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany.
authors: Antonia
authors: A
authors: Albers
authors: Serhiy
authors: S
authors: Demeshko
authors: Kevin
authors: K
authors: Pröpper
authors: Sebastian
authors: S
authors: Dechert
authors: Eckhard
authors: E
authors: Bill
authors: Franc
authors: F
authors: Meyer
mesh_terms: D018360:Crystallography, X-Ray; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D015204:Spectroscopy, Mossbauer
chemical_list: D007506:Iron-Sulfur Proteins