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论文类型：期刊论文

发表时间：2013-09-14

发表刊物：DALTON TRANSACTIONS

收录刊物：SCIE、EI、PubMed、Scopus

卷号：42

期号：34

页面范围：12059-12071

ISSN号：1477-9226

摘要：[FeFe]-hydrogenases are enzymes in nature that catalyze the reduction of protons and the oxidation of H-2 at neutral pH with remarkably high activities and incredibly low overpotential. Structural and functional biomimicking of the active site of [FeFe]-hydrogenases can provide helpful hints for elucidating the mechanism of H-2 evolution and uptake at the [FeFe]-hydrogenase active site and for designing bio-inspired catalysts to replace the expensive noble metal catalysts for H-2 generation and uptake. This perspective focuses on the recent progress in the formation and reactivity of iron hydrides closely related to the processes of proton reduction and hydrogen oxidation mediated by diiron dithiolate complexes. The second section surveys the bridging and terminal hydride species formed from various diiron complexes as well as the intramolecular proton transfer. The very recent progress in H-2 activation by diiron dithiolate models are reviewed in the third section. In the concluding remarks and outlook, the differences in structure and catalytic mechanism between the synthetic models and the native [FeFe]-H(2)ase active site are compared and analyzed, which may cause the need for a significantly larger driving force and may lead to lower activities of synthetic models than the [FeFe]-H(2)ases for H-2 generation and uptake.