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Issue 42, 2012

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

Author affiliations

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

Supplementary files

Article information


Submitted
10 Feb 2012
Accepted
27 Mar 2012
First published
28 Mar 2012

Dalton Trans., 2012,41, 13112-13119
Article type
Paper

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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