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Issue 14, 2018
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Intramolecular stabilization of a catalytic [FeFe]-hydrogenase mimic investigated by experiment and theory

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Abstract

The mono-substituted complex [Fe2(CO)5(μ-naphthalene-2-thiolate)2(P(PhOMe-p)3)] was prepared taking after the structural principles from both [NiFe] and [FeFe]-hydrogenase enzymes. Crystal structures are reported for this complex and the all carbonyl analogue. The bridging naphthalene thiolates resemble μ-bridging cysteine amino acids. One of the naphthyl moieties forms π–π stacking interactions with the terminal bulky phosphine ligand in the crystal structure and in calculations. This interaction stabilizes the reduced and protonated forms during electrocatalytic proton reduction in the presence of acetic acid and hinders the rotation of the phosphine ligand. The intramolecular π–π stabilization, the electrochemistry and the mechanism of the hydrogen evolution reaction were investigated using computational approaches.

Graphical abstract: Intramolecular stabilization of a catalytic [FeFe]-hydrogenase mimic investigated by experiment and theory

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Publication details

The article was received on 21 Dec 2017, accepted on 26 Feb 2018 and first published on 27 Feb 2018


Article type: Paper
DOI: 10.1039/C7DT04837H
Citation: Dalton Trans., 2018,47, 4941-4949
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    Intramolecular stabilization of a catalytic [FeFe]-hydrogenase mimic investigated by experiment and theory

    I. K. Pandey, M. Natarajan, H. Faujdar, F. Hussain, M. Stein and S. Kaur-Ghumaan, Dalton Trans., 2018, 47, 4941
    DOI: 10.1039/C7DT04837H

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