title: Hydrogen activation by biomimetic diiron dithiolates.
abstract: Using the thermally stable salts of [Fe(2)(SR)(2)(CO)(3)(PMe(3))(dppv)]BAr(F)(4), we found that the azadithiolates [Fe(2)(adtR)(CO)(3)(PMe(3))(dppv)](+) react with high pressures of H(2) to give the hydride [Fe(2)(mu-H)(adtR)(CO)(3)(dppv)(PMe(3))]BAr(F)(4). The related oxadithiolate and propanedithiolate complexes are unreactive toward H(2). Molecular hydrogen is proposed to undergo heterolysis assisted by the amine followed by isomerization of an initially formed terminal hydride. Use of H(2) and D(2)O gave the deuteride as well as the hydride, implicating protic intermediates.
authors: Department of Chemistry, University of Illinois, Urbana, Illinois 61801, USA.
authors: Matthew T
authors: MT
authors: Olsen
authors: Bryan E
authors: BE
authors: Barton
authors: Thomas B
authors: TB
authors: Rauchfuss
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism; D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry* / Q000378:metabolism; D006864:Hydrogenase / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D005290:Ferric Compounds; D007506:Iron-Sulfur Proteins; D013438:Sulfhydryl Compounds; C002007:dithiol-iron(III)-sulfide complex; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase