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Molecular enzymology of a novel tetrathionate reductase

Reference	B19923
Principal Investigator / Supervisor	Professor Graeme Reid
Co-Investigators / Co-Supervisors	Professor Stephen Chapman, Dr Christopher Mowat
Institution	University of Edinburgh
Department	Inst of Cell and Molecular Biology
Funding type	Research
Value (£)	229,810
Status	Completed
Type	Research Grant
Start date	01/10/2003
End date	30/09/2006
Duration	36 months

Abstract

We have identified a novel tetrathionate reductase from the bacterium Shewanella oneidensis. The enzyme is located in the bacterial periplasm and contains 8 covalently-attached heme groups. We have purified the protein and determined its crystal structure allowing us now to undertake a detailed investigation of electron transfer and catalysis in this remarkable enzyme using a variety of approaches. Spectroscopic and redox studies will focus on the electronic properties of the heme cofactors. Site-directed mutagenesis will allow us to identify the roles of amino acid side chains in enzymatic activity. In all of this work, X-ray crystallography will enable us to correlate structural details with substrate binding and catalytic function.

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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