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Defining substrate binding specificity in ascorbate peroxidase

ReferenceB19083
Principal Investigator / Supervisor Professor Emma Raven
Co-Investigators /
Co-Supervisors
Institution University of Leicester
DepartmentChemistry
Funding typeResearch
Value (£) 207,908
StatusCompleted
TypeResearch Grant
Start date 19/05/2003
End date 19/05/2006
Duration36 months

Abstract

We seek a complete description of the substrate binding specificity in ascorbate peroxidase (APX). APX is an excellent model for probing these questions since its substrate binding properties are diverse and place it at the interface between the class I and class III haem peroxidases. The specific aims are: (i) to probe binding of ascorbate at the gamma-meso haem position; (ii) to identify the location of the second ascorbate binding site in APX; (iii) to examine the role of hydrophobic interactions in determining aromatic substrate binding affinity and (iv) to engineer a cytochrome c binding site into APX. The information will underpin our general understanding of the different functional activities exhibited by the haem peroxidases.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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