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Issue 34, 2013
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Reactions of [FeFe]-hydrogenase models involving the formation of hydrides related to proton reduction and hydrogen oxidation

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Abstract

[FeFe]-hydrogenases are enzymes in nature that catalyze the reduction of protons and the oxidation of H2 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 H2 evolution and uptake at the [FeFe]-hydrogenase active site and for designing bioinspired catalysts to replace the expensive noble metal catalysts for H2 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 H2 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]-H2ase 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]-H2ases for H2 generation and uptake.

Graphical abstract: Reactions of [FeFe]-hydrogenase models involving the formation of hydrides related to proton reduction and hydrogen oxidation

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Publication details

The article was received on 27 May 2013, accepted on 19 Jun 2013 and first published on 20 Jun 2013


Article type: Perspective
DOI: 10.1039/C3DT51371H
Citation: Dalton Trans., 2013,42, 12059-12071
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    Reactions of [FeFe]-hydrogenase models involving the formation of hydrides related to proton reduction and hydrogen oxidation

    N. Wang, M. Wang, L. Chen and L. Sun, Dalton Trans., 2013, 42, 12059
    DOI: 10.1039/C3DT51371H

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