Award details

The structural and mechanistic mapping of a unique fumarate reductase

ReferenceB07650
Principal Investigator / Supervisor Professor Stephen Chapman
Co-Investigators /
Co-Supervisors
Professor Graeme Reid, Professor Malcolm Walkinshaw
Institution University of Edinburgh
DepartmentSch of Chemistry
Funding typeResearch
Value (£) 178,365
StatusCompleted
TypeResearch Grant
Start date 01/04/1997
End date 01/04/2000
Duration36 months

Abstract

The fumarate reductase from Shewanella putrefaciens is a unique flavo-haemo-enzyme. In contrast to the typical membrane bound fumarate reductases from other microorganisms, the S. putrefaciens enzyme is structurally simpler, soluble, and available in large amounts. This makes it immensely valuable for structural and functional studies. We shall therefore: i) Determine the X-ray crystal structure of the enzyme; ii) Provide recombinant wild-type and mutant forms of the enzyme in sufficient quantities for full structure/function analysis; and iii) Determine the exact catalytic mechanism of the enzyme at a molecular level .

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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