Abstract
As the biomimetic models of [FeFe]-hydrogenase active sites, two new di- and mononuclear iron complexes with chelating PNP ligands (PNP = (Ph2P)2NR) have been prepared and structurally determined by single-crystal X-ray diffraction analysis. Treatment of precursor Fe2(μ-edt)(CO)6 (A, edt = SCH2CH2S) with diphosphine (Ph2P)2N(CHMe2) in the presence of Me3NO·2H2O in MeCN produced a dinuclear iron complex Fe(μ-edt)(CO)4{κ2 -(Ph2P)2N(CHMe2)} (1), whereas the similar reaction of Fe2(μ-odt)(CO)6 (B, odt = SCH2OCH2S) with (Ph2P)2N(CH2)3Me afforded a mononuclear iron complex Fe(κ2 -odt)(CO)2{κ2 -(Ph2P)2N(CH2)3Me} (2). The crystal structure of 1 contains a butterfly [Fe2S2] cluster, whereas that of 2 exhibits a square bipyramidal geometry of Fe atom.
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