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

Pim W.J.M. Frederix, Rafal Kania, Joseph A. Wright, Dimitrios A. Lamprou, Rein V. Ulijn, Christopher J. Pickett, Neil T. Hunt*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)
39 Downloads (Pure)

Abstract

A [FeFe]-hydrogenase model compound (-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.

Original languageEnglish
Pages (from-to)13112-13119
Number of pages8
JournalDalton Transactions
Volume41
Issue number42
Early online date28 Mar 2012
DOIs
Publication statusPublished - 14 Nov 2012
Externally publishedYes

ASJC Scopus subject areas

  • Inorganic Chemistry

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