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Details of Grant 

EPSRC Reference: GR/R47547/01
Title: Investigation of metal bound sulfur radical chemistry; implication fro stabilised thiyl radicals in biology
Principal Investigator: Archibald, Professor S
Other Investigators:
Researcher Co-Investigators:
Project Partners:
Department: Chemistry
Organisation: University of Hull
Scheme: Fast Stream
Starts: 01 October 2002 Ends: 30 September 2005 Value (£): 62,346
EPSRC Research Topic Classifications:
Chemical Synthetic Methodology Co-ordination Chemistry
EPSRC Industrial Sector Classifications:
Pharmaceuticals and Biotechnology No relevance to Underpinning Sectors
Related Grants:
Panel History:  
Summary on Grant Application Form
More and more examples of radical species as essential co-factors to enzymes are being determined. Metal bound phenoxyl radicals, observed in the catalytic cycle of galactose oxidase, have been a successful target for biomimicry studies resulting in functional catalysts.Thiyl radicals have been shown to be an intermediate in nucleotide reduction by ribonucleoside triphosphate reductase from Lactobacillus leichmanii. It can be anticipated that in some metalloenzymes, where the metal has a sulfur rich coordination sphere and redox processes are occurring, a stabilised metal bound thiyl radical may be involved in catalytic pathways.Charactyerisation of this type of species in a model system is proposed using a novel molecular building block to stabilise phenylthiyl radicals in an analogous manner to the already well developed metal bound phenoxyl and anilinyl radical compunds.Preliminary studies with new ligands which combine a thiolate donor into the same ligand as a thiophenolate will allow observation of the oxidation processes forming sulfenate groups, through to have an esssential role in enzyme activity control.
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Organisation Website: http://www.hull.ac.uk