Award details

The crystallographic and kinetic delineation of the catalytic mechanism in fumarate reductase

ReferenceB13402
Principal Investigator / Supervisor Professor Malcolm Walkinshaw
Co-Investigators /
Co-Supervisors
Professor Stephen Chapman, Professor Graeme Reid
Institution University of Edinburgh
DepartmentInst of Cell and Molecular Biology
Funding typeResearch
Value (£) 174,088
StatusCompleted
TypeResearch Grant
Start date 01/10/2000
End date 01/10/2003
Duration36 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 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
terms and conditions of use (opens in new window)
export PDF file