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Issue 30, 2017
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A mononuclear iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] with bulky phosphine ligands: a model for the [FeFe] hydrogenase enzyme active site with an inverted redox potential

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Abstract

A mononuclear hexa-coordinated iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] 1 (bdt = 1,2-benzenedithiolate; PTA = 1,3,5-triaza-7-phosphaadamantane) with two bulky phosphine ligands in the trans position was synthesized and characterized by X-ray structural analysis coulometry data, FTIR, electrochemistry and electronic structure calculations. The complex undergoes a facilitated two-electron reduction 1/12− and shows an inverted one-electron reduction for 1/1 at higher potentials. Electrochemical investigations of 1 are compared to the closely related [Fe(bdt)(CO)2(PMe3)2] compound. A mechanistic suggestion for the hydrogen evolution reaction upon proton reduction from acid media is derived. The stability of 1 in both weak and strong acids is monitored by cyclic voltammetry.

Graphical abstract: A mononuclear iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] with bulky phosphine ligands: a model for the [FeFe] hydrogenase enzyme active site with an inverted redox potential

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Supplementary files

Article information


Submitted
01 Jun 2017
Accepted
04 Jul 2017
First published
10 Jul 2017

This article is Open Access

Dalton Trans., 2017,46, 10050-10056
Article type
Paper

A mononuclear iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] with bulky phosphine ligands: a model for the [FeFe] hydrogenase enzyme active site with an inverted redox potential

M. Natarajan, H. Faujdar, S. M. Mobin, M. Stein and S. Kaur-Ghumaan, Dalton Trans., 2017, 46, 10050
DOI: 10.1039/C7DT01994G

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