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The mechanism of action of lignin peroxidase: towards designer substrate oxidation sites

ReferenceB11934
Principal Investigator / Supervisor Professor Andrew Trevor Smith
Co-Investigators /
Co-Supervisors
Dr Christopher Davies, Dr Wendy Doyle
Institution University of Sussex
DepartmentSch of Life Sciences
Funding typeResearch
Value (£) 190,592
StatusCompleted
TypeResearch Grant
Start date 01/09/1999
End date 01/01/2003
Duration40 months

Abstract

Understanding of the catalytic mechanism of lignin peroxidase has been greatly facilitated by the discovery of a unique substrate oxidation site involving the redox active side chain of W171 and long-range electron transfer to the haem. We will: (i) investigate the role of the negatively charged environment of W171 in the oxidation of veratryl alcohol (ii), test a putative electron transfer pathway to the haem and (iii) investigate the role of residues controlling the access of larger substrates to the classical haem-edge substrate interaction site. Physical and kinetic studies of specific mutants will be complemented by their structure determination by X-ray crystallography.

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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