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The structural and mechanistic mapping of a unique fumarate reductase
Reference
B07650
Principal Investigator / Supervisor
Professor Stephen Chapman
Co-Investigators /
Co-Supervisors
Professor Graeme Reid
,
Professor Malcolm Walkinshaw
Institution
University of Edinburgh
Department
Sch of Chemistry
Funding type
Research
Value (£)
178,365
Status
Completed
Type
Research Grant
Start date
01/04/1997
End date
01/04/2000
Duration
36 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 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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