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

Pim Frederix, Rafal Kania, Joseph A. Wright, Dimitrios Lamprou, Rein Ulijn, Christopher J. Pickett, Neil Hunt

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)


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 centers 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
Issue number42
Early online date28 Mar 2012
Publication statusPublished - 12 Oct 2012


  • [FeFe]-hydrogenase model compound
  • peptide hydrogels
  • stability
  • photochemistry
  • chemical environment
  • encapsulated molecules
  • solution phase systems
  • artificial hydrogenases


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