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Metal Complexes Relating to Enzymes of the Nitrogen Cycle

Reference	BBS/E/J/40004057
Principal Investigator / Supervisor	Dr Raymond Richards
Co-Investigators / Co-Supervisors	Dr David Hughes
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	149,899
Status	Completed
Type	Institute Project
Start date	01/04/1997
End date	31/03/2001
Duration	48 months

Abstract

This project uses metal complexes to aid in understanding the function at the atomic level of nitrite reductase, nitrate reductase and other key metallo- enzymes of the nitrogen cycle with the exclusion of nitrogenase. The project mainly concerns denitrification, whereby bacteria remove nitrogen oxides from their environment, ultimately as dinitrogen. Copper-based nitrite reductase mediates the transformation of NO2- to NO and N2O and contains copper in so- called Type 1 and Type 2 centres, the latter is the active site at which nitrite is reduced. Model complexes for both copper centres are being synthesised to develop understanding of biological nitrite reduction with a view to designing new catalysts for the removal of nitrogen oxides from the environment. Similar studies will help elucidate the function of NO and N2O reductases. Nitrate reductase catalyses the reduction of NO3- to NO2- using a single molybdenum centre with oxide and pterin ligation (Moco). Insight on the function of Moco will be obtained by study of the reactions of NO3- at molybdenum complexes having appropriate sulphur-ligand and oxide ligation. This interdisciplinary project interfaces with RO 4051

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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