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Dalton Trans. 2012 Nov 14;41(42):13112-9. doi: 10.1039/c2dt30307h.

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

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  • 1Department of Physics, University of Strathclyde, SUPA, Glasgow, UK.

Abstract

A [FeFe]-hydrogenase model compound (ยต-S(CH(2))(3)S)Fe(2)(CO)(4)(PMe(3))(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.

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