Picture of DNA strand

Pioneering chemical biology & medicinal chemistry through Open Access research...

Strathprints makes available scholarly Open Access content by researchers in the Department of Pure & Applied Chemistry, based within the Faculty of Science.

Research here spans a wide range of topics from analytical chemistry to materials science, and from biological chemistry to theoretical chemistry. The specific work in chemical biology and medicinal chemistry, as an example, encompasses pioneering techniques in synthesis, bioinformatics, nucleic acid chemistry, amino acid chemistry, heterocyclic chemistry, biophysical chemistry and NMR spectroscopy.

Explore the Open Access research of the Department of Pure & Applied Chemistry. Or explore all of Strathclyde's Open Access research...

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

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 1477-9234

Full text not available in this repository. Request a copy from the Strathclyde author

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 centers is likely to be crucial in exploiting artificial hydrogenases, these gels may offer a new option for future materials design involving catalysts.