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Molecular basis for catalysis in copper-containing oxidases: X-ray crystallographic studies

Reference	B10432
Principal Investigator / Supervisor	Professor Simon Phillips
Co-Investigators / Co-Supervisors	Professor Peter Knowles, Professor Michael McPherson
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	231,784
Status	Completed
Type	Research Grant
Start date	08/03/1999
End date	08/07/2002
Duration	40 months

Abstract

Despite the fundamental importance of oxygen activation and utilisation in biology, we do not understand the chemistry of these processes, and particularly how metal ions are involved. A full description of the mechanism of any enzyme should include complete characterisation of the structure and chemistry of the intermediates. In copper-containing amine oxidase, the catalytic mechanism can be considered as a reductive half-cycle, in which the active, oxidised enzyme binds substrate amine and converts if to product aldehyde, and an oxidative half cycle, where molecular oxygen binds to the reduced enzyme and reactivates it. We plan to trap catalytic intermediates in amine oxidase crystals under appropriate conditions by rapid freezing to cryogenic temperatures, monitored by real-time single crystal spectrophotometry, and determine the structures by X-ray crystallography. The ultimate aim is to generate a 'movie' of the catalytic cycle, that should lead, in conjunction with dynamic information from solution techniques, to a full understanding of the chemistry of catalysis.

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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