Synthesis and reactivity of iron acyl complexes modeling the active site of [Fe]-hydrogenase.
A [Fe(II)Fe(II)] dithiolate complex containing acyl and carbonyl ligands was synthesized. The diiron complex reacted with phosphine, cyanide, isocyanide, and CO to give monomeric Fe(II) complexes reproducing the first coordination sphere of the active site of [Fe]-hydrogenase (H(2)-forming methylene-tetrahydromethanopterin dehydrogenase, Hmd) in various states. All the acyl and carbonyl carbons in the diiron complex underwent facile isotopic exchange with (13)CO via monomeric Fe tricarbonyl intermediates.
Chen
Dafa
D
Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, SB-ISIC-LSCI, BCH 3305, Lausanne 1015, Switzerland.
Scopelliti
Rosario
R
Hu
Xile
X
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005290:Ferric Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008968:Molecular Conformation
D005290:Ferric Compounds; D007506:Iron-Sulfur Proteins; C118830:iron hydrogenase; D006864:Hydrogenase