EPSRC logo

Details of Grant 

EPSRC Reference: GR/R65916/01
Title: The Electronic Structure of the Active Sites of Oxomolybdo-and Oxotungstoenzymes.
Principal Investigator: McMaster, Professor J
Other Investigators:
Researcher Co-Investigators:
Project Partners:
University of Nottingham
Department: Sch of Chemistry
Organisation: University of Nottingham
Scheme: Fast Stream
Starts: 23 September 2002 Ends: 22 September 2005 Value (£): 62,897
EPSRC Research Topic Classifications:
Biological & Medicinal Chem. Chemical Biology
Chemical Structure
EPSRC Industrial Sector Classifications:
Electronics No relevance to Underpinning Sectors
Related Grants:
Panel History:  
Summary on Grant Application Form
Molybdenum and tungsten are unique in being the only 4d (Mo) and 5d (W) transition metals that are required for the normal metabolism of biological systems; indeed, Mo is required as a trace element by all forms of life. Mo is at the active centre of more than thirty redox enzymes that catalyse key reactions in the metabolism of C, N, and S of microorganisms, plants, animals, and humans. In each case, X-ray crystallography has confirmed that the metal is co-ordinated to the ene-1,2-dithiolate (or dithiolene) group of a special pterin, molybdopterin (MPT). However, the role of this special ligation in controlling the chemistry of these important enzymes remains to be defined.The research will evaluate key roles for MPT through extensive spectroscopic studies on new small molecule analogues of the active sites of Mo and W eznymes on the native and W-substituted DMSO reductases from Rhodobacter capsulatus. We will employ magnetic circular dichroism (MCD) spectroscopy that is an extremely powerful technique for probing the electronic structure of paramagnetic metal centres and develop frameworks to interpret the spectroscopic data using density functional theory. Our description of the electronic structure of these centres will enable an evaluation of the possible roles for MPT in controlling the catalysis achieved by the Mo and W enzymes.
Key Findings
This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
Potential use in non-academic contexts
This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
Impacts
Description This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
Summary
Date Materialised
Sectors submitted by the Researcher
This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
Project URL:  
Further Information:  
Organisation Website: http://www.nottingham.ac.uk