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Structural studies on the novel multicopper enzyme nitrous oxide reductase; a key enzyme of the nitrogen cycle

Reference	B07079
Principal Investigator / Supervisor	Professor Stuart John Ferguson
Co-Investigators / Co-Supervisors	Professor Benjamin Berks, Professor Robert Conlan
Institution	University of Oxford
Department	Biochemistry
Funding type	Research
Value (£)	190,355
Status	Completed
Type	Research Grant
Start date	01/02/1997
End date	01/05/2001
Duration	51 months

Abstract

We will obtain a 2.5 Angstroms structure of the multicopper enzyme nitrous oxide reductase using highly diffracting crystals recently grown by us. N2O reductase is a key component of the nitrogen cycle. The active site contains a novel, but poorly characterised, copper- containing cofactor. N2O reductase also binds a binuclear CuA centre of the type found in cytochrome c oxidase. Structural comparisons of the two CuA-sites will contribute to defining the function of the unusual electron transfer centre. We will clone and sequence the N2O reductase structural gene to enable determination of the enzyme structure. We shall initiate site-directed mutagenesis studies to investigate enzyme mechanism in the light of the structural information obtained, as well as to probe the role of the unusual periplasmic targeting sequence associated with this protein.

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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