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The crystallographic and kinetic delineation of the catalytic mechanism in fumarate reductase
Reference
B13402
Principal Investigator / Supervisor
Professor Malcolm Walkinshaw
Co-Investigators /
Co-Supervisors
Professor Stephen Chapman
,
Professor Graeme Reid
Institution
University of Edinburgh
Department
Inst of Cell and Molecular Biology
Funding type
Research
Value (£)
174,088
Status
Completed
Type
Research Grant
Start date
01/10/2000
End date
01/10/2003
Duration
36 months
Abstract
We have solved the X-ray crystal structure of the S. frigidimarina fumarate reductase to 1.8 Angstrom resolution. This has allowed us to propose a detailed mechanism for fumarate reduction. We shall now build on this work by testing the proposed mechanism using a combination of site- directed mutagenesis, solution studies and X-ray crystallography. The crystallography will include inhibitor-bound structures and mutant enzyme structures. In addition, anaerobic crystallography will be used to examine the structure of the enzymes in the reduced as well as oxidised form. We believe this work will have important implications for all members of this important family of enzymes.
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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