Synthesis and structural characterization of the mono- and diphosphine-containing diiron propanedithiolate complexes related to [FeFe]-hydrogenases. Biomimetic H2 evolution catalyzed by (mu-PDT)Fe2(CO)4[(Ph2P)2N(n-Pr) |
| |
Authors: | Song Li-Cheng Li Chang-Gong Ge Jian-Hua Yang Zhi-Yong Wang Hu-Ting Zhang Juan Hu Qing-Mei |
| |
Institution: | Department of Chemistry, State Key Laboratory of Elemento-Organic Chemistry, Nankai University, Tianjin 300071, China |
| |
Abstract: | As the new H-cluster models, six diiron propanedithiolate (PDT) complexes with mono- and diphosphine ligands have been prepared and structurally characterized. The monophosphine model complex (μ-PDT)Fe2(CO)5Ph2PNH(t-Bu)] (1) was prepared by reaction of parent complex (μ-PDT)Fe2(CO)6 (A) with 1 equiv of Ph2PNH(t-Bu) in refluxing xylene, whereas A reacted with 1 equiv of Me3NO · 2H2O in MeCN at room temperature followed by 1 equiv of Ph2PH to give the corresponding monophosphine model complex (μ-PDT)Fe2(CO)5(Ph2PH) (2). Further treatment of 2 with 1 equiv of n-BuLi in THF at −78 °C followed by 1 equiv of CpFe(CO)2I from −78 °C to room temperature afforded monophosphine model complex (μ-PDT)Fe2(CO)5Ph2PFe(CO)2Cp] (3), whereas the diphosphine model complexes (μ-PDT)Fe2(CO)4(Ph2PC2H4PPh2) (4), (μ-PDT)Fe2(CO)4(Ph2P)2N(n-Pr)] (5) and (μ-PDT)Fe2(CO)4(Ph2P)2N(n-Bu)] (6) were obtained by reactions of A with ca.1 equiv of the corresponding diphosphines in refluxing xylene. All the new model complexes were characterized by elemental analysis, spectroscopy and particularly for 1 and 3-6 by X-ray crystallography. On the basis of electrochemical and spectroelectrochemical studies, model 5 was found to be a catalyst for HOAc proton reduction to H2, and for this electrocatalytic reaction an ECCE mechanism was proposed. |
| |
Keywords: | Hydrogenase enzyme Diiron propanedithiolate Phosphine ligand Enzyme model H2 production |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|