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Protein processing and electron transfer in the radical copper enzyme galactose oxidase: protein and model studies

Reference	B11662
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 (£)	165,790
Status	Completed
Type	Research Grant
Start date	01/11/1999
End date	01/05/2003
Duration	42 months

Abstract

Recently several metalloenzymes have been shown to possess oxidatively modified or bridged amino acids at their active sites. For amine oxidases, formation of the trihydroxyphenylamine quinone (TPQ) cofactor from tryrosine has been shown to be an oxygen and copper-dependent autocatalytic process. The role of oxygen and copper in the formation of the thioether bridge at the active site of the radical copper-containing galactose oxidase will be explored by protein chemistry, mutagenic and synthetic chemistry approaches. Related autocatalytic processing of the pro- to mature enzyme will also be investigated. The existence of an electron transfer pathway from a surface disulphide to the radical site will be explored by mutagenesis and protein chemistry and the relationship between this pathway and the protein processing events will be defined.

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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