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Molecular basis for catalysis in copper-containing oxidases: the oxidative half reaction

Reference	B13477
Principal Investigator / Supervisor	Professor Michael McPherson
Co-Investigators / Co-Supervisors	Professor Malcolm Halcrow, Professor Peter Knowles, Professor Simon Phillips
Institution	University of Leeds
Department	Plant Biochemistry & Biotechnology
Funding type	Research
Value (£)	231,692
Status	Completed
Type	Research Grant
Start date	01/06/2001
End date	01/06/2004
Duration	36 months

Abstract

Despite its fundamental importance in biology we have a poor understanding of the mechanisms of oxygen activation and utilisation. In some metalloenzymes the metal has been shown to be responsible for modifying amino acid residues in the enzyme to form novel organic cofactors thereby conferring new catalytic potential for effecting difficult chemistry such as C-H bond cleavage and oxygen activation processes. Amine oxidases offer an ideal system to explore this new chemistry. We have made remarkable progress recently on cryocrystallography of trapped intermediates in the E. coli amine oxidase (ECAO; Science, In Press). This proposal takes these studies as a basis for solution and spectroscopic studies of wild-type and mutational variant forms of ECAO to elucidate key aspects of oxygen activation and reduction in the catalytic cycle.

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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