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Thionate-reducing molybdoenzymes from an enteric bacterium
Reference
BCI05147
Principal Investigator / Supervisor
Professor Benjamin Berks
Co-Investigators /
Co-Supervisors
Institution
University of East Anglia
Department
Biological Sciences
Funding type
Research
Value (£)
147,102
Status
Completed
Type
Research Grant
Start date
01/01/1996
End date
01/01/1999
Duration
36 months
Abstract
Enzymes involved in the reduction of thionate compounds are currently poorly characterised at the molecular level. The molybdopterin-dependent tetrathionate reductase of Salmonella typhimurium LT2 will be studied using a combination of biochemical, genetic and spectroscopic techniques. The molybdopterin cofactor normally carries out reactions involving oxygen atom transfer. The possibility that the molybdopterin cofactor in tetrathionate reductase catalyses a physiologically novel sulphur atom transfer reaction will be investigated. Our proposal that the endothermic reduction of thiosulphate by menaquinol in S. typhimurium is driven by the protonmotive force will be tested.
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
Biological Chemistry Initiative (BCI) [1995]
Funding Scheme
X – not Funded via a specific Funding Scheme
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