Computational Investigation of [FeFe]-Hydrogenase Models: Characterization of Singly and Doubly Protonated Intermediates and Mechanistic Insights

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• 作者：Mioy T. Huynh ; Wenguang Wang ; Thomas B. Rauchfuss ; Sharon Hammes-Schiffer
• 刊名：Inorganic Chemistry
• 出版年：2014
• 出版时间：October 6, 2014
• 年：2014
• 卷：53
• 期：19
• 页码：10301-10311
• 全文大小：568K
• ISSN：1520-510X

文摘

The [FeFe]-hydrogenase enzymes catalyze hydrogen oxidation and production efficiently with binuclear Fe metal centers. Recently the bioinspired H₂-producing model system Fe₂(adt)(CO)₂(dppv)₂ (adt=azadithiolate and dppv=diphosphine) was synthesized and studied experimentally. In this system, the azadithiolate bridge facilitates the formation of a doubly protonated ammonium-hydride species through a proton relay. Herein computational methods are utilized to examine this system in the various oxidation states and protonation states along proposed mechanistic pathways for H₂ production. The calculated results agree well with the experimental data for the geometries, CO vibrational stretching frequencies, and reduction potentials. The calculations illustrate that the NH路路路HFe dihydrogen bonding distance in the doubly protonated species is highly sensitive to the effects of ion-pairing between the ammonium and BF₄^{鈥?/sup> counterions, which are present in the crystal structure, in that the inclusion of BF₄鈥?/sup> counterions leads to a significantly longer dihydrogen bond. The non-hydride Fe center was found to be the site of reduction for terminal hydride species and unsymmetric bridging hydride species, whereas the reduced symmetric bridging hydride species exhibited spin delocalization between the Fe centers. According to both experimental measurements and theoretical calculations of the relative pK_a values, the Fe_d center of the neutral species is more basic than the amine, and the bridging hydride species is more thermodynamically stable than the terminal hydride species. The calculations implicate a possible pathway for H₂ evolution that involves an intermediate with H₂ weakly bonded to one Fe, a short H₂ distance similar to the molecular bond length, the spin density delocalized over the two Fe centers, and a nearly symmetrically bridged CO ligand. Overall, this study illustrates the mechanistic roles of the ammonium-hydride interaction, flexibility of the bridging CO ligand, and intramolecular electron transfer between the Fe centers in the catalytic cycle. Such insights will assist in the design of more effective bioinspired catalysts for H₂ production.}