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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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Supplementary files

Article information


Submitted
21 Dec 2017
Accepted
26 Feb 2018
First published
27 Feb 2018

This article is Open Access

Dalton Trans., 2018,47, 4941-4949
Article type
Paper

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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