Frederix, Pim and Kania, Rafal and Wright, Joseph A. and Lamprou, Dimitrios and Ulijn, Rein and Pickett, Christopher J. and Hunt, Neil (2012) Encapsulating [FeFe]-hydrogenase model compounds in peptide hydrogels dramatically modifies stability and photochemistry. Dalton Transactions, 41 (42). pp. 13112-13119. ISSN 1472-7773Full text not available in this repository. (Request a copy from the Strathclyde author)
A [FeFe]-hydrogenase model compound (µ-S(CH2)3S)Fe2(CO)4(PMe3)2  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.
|Keywords:||[FeFe]-hydrogenase model compound , peptide hydrogels , stability , photochemistry , chemical environment , encapsulated molecules, solution phase systems, artificial hydrogenases, Physics, Pharmacy and materia medica, Chemistry|
|Subjects:||Science > Physics|
Medicine > Pharmacy and materia medica
Science > Chemistry
|Department:||Faculty of Science > Physics|
Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
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Faculty of Science > Pure and Applied Chemistry
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|Depositing user:||Pure Administrator|
|Date Deposited:||11 Sep 2012 13:53|
|Last modified:||13 Jun 2013 09:45|
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