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Mimicking the active site of chloroperoxidase with distal pocket mutants of horseradish peroxidase

Reference	B17590
Principal Investigator / Supervisor	Professor Andrew Trevor Smith
Co-Investigators / Co-Supervisors	Dr Nigel Brissett
Institution	University of Sussex
Department	Sch of Life Sciences
Funding type	Research
Value (£)	193,444
Status	Completed
Type	Research Grant
Start date	01/05/2002
End date	01/05/2005
Duration	36 months

Abstract

A number of distal pocket mutants of horseradish peroxidase (HRP) have been constructed in order to mimic the open active site of chloroperoxidase, an enzyme which has both peroxidase and peroxygenase (P450-like) activity. One of these, HRP H42E:F41A:R38H has a very high styrene epoxidation activity. We will (i) determine the high resolution crystal structure of this and other mutants with enhanced conventional peroxidase activity (ii) probe the interaction of substrates with the engineered haem cavity, by both crystallographic and NMR methods (iii) investigate in detail the nature of the catalytic intermediates responsible for peroxygenase activity and (iv) construct additional mutants building on present knowledge to further extend this engineering approach.

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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