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Issue 42, 2012
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Encapsulating [FeFe]-hydrogenase model compounds in peptide hydrogels dramatically modifies stability and photochemistry

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Abstract

A [FeFe]-hydrogenase model compound (µ-S(CH2)3S)Fe2(CO)4(PMe3)2 [1] has been encapsulated in a low molecular weight (LMW) hydrogelator (Fmoc–Leu–Leu). Linear infrared absorption spectroscopy, gel melting and ultrafast time-resolved infrared spectroscopy experiments reveal significant contrasts in chemical environment and photochemistry between the encapsulated molecules and solution phase systems. Specifically, the gel provides a more rigid hydrogen bonding environment, which restricts isomerisation following photolysis while imparting significant increases in stability relative to a similarly aqueous solution. Since understanding and ultimately controlling the mechanistic role of ligands near Fe centres is likely to be crucial in exploiting artificial hydrogenases, these gels may offer a new option for future materials design involving catalysts.

Graphical abstract: Encapsulating [FeFe]-hydrogenase model compounds in peptide hydrogels dramatically modifies stability and photochemistry

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Publication details

The article was received on 10 Feb 2012, accepted on 27 Mar 2012 and first published on 28 Mar 2012


Article type: Paper
DOI: 10.1039/C2DT30307H
Citation: Dalton Trans., 2012,41, 13112-13119
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    Encapsulating [FeFe]-hydrogenase model compounds in peptide hydrogels dramatically modifies stability and photochemistry

    P. W. J. M. Frederix, R. Kania, J. A. Wright, D. A. Lamprou, R. V. Ulijn, C. J. Pickett and N. T. Hunt, Dalton Trans., 2012, 41, 13112
    DOI: 10.1039/C2DT30307H

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