EPSRC Reference: |
GR/R65916/01 |
Title: |
The Electronic Structure of the Active Sites of Oxomolybdo-and Oxotungstoenzymes. |
Principal Investigator: |
McMaster, Professor J |
Other Investigators: |
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Researcher Co-Investigators: |
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Project Partners: |
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Department: |
Sch of Chemistry |
Organisation: |
University of Nottingham |
Scheme: |
Fast Stream |
Starts: |
23 September 2002 |
Ends: |
22 September 2005 |
Value (£): |
62,897
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EPSRC Research Topic Classifications: |
Biological & Medicinal Chem. |
Chemical Biology |
Chemical Structure |
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EPSRC Industrial Sector Classifications: |
Electronics |
No relevance to Underpinning Sectors |
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Related Grants: |
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Panel History: |
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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.
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Key Findings |
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Potential use in non-academic contexts |
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Impacts |
Description |
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Summary |
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Date Materialised |
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Sectors submitted by the Researcher |
This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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Project URL: |
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Further Information: |
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Organisation Website: |
http://www.nottingham.ac.uk |