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X-ray structure of the catalytic component of benzene dioxygenase
Reference
BCI06226
Principal Investigator / Supervisor
Professor Brian Sutton
Co-Investigators /
Co-Supervisors
Professor Jeremy Richard Mason
Institution
King's College London
Department
GKT School of Biomedical Sciences
Funding type
Research
Value (£)
184,976
Status
Completed
Type
Research Grant
Start date
01/09/1996
End date
01/09/1999
Duration
36 months
Abstract
We shall determine the X-ray structure of the iron-sulphur protein component of benzene dioxygenase. Suitable crystals are available. The enzyme catalyses the cis hydroxylation of aromatic substrates, and has applications in hazardous waste detoxification, and in biotransformations for enantiospecific synthesis. This reaction has no chemical synthetic equivalent. X-ray structures of substrate complexes will be determined. The corresponding component of toluene dioxygenase will be crystallised and its structure determined by molecular replacement. Knowledge of one or both of these structures will provide a basis for mechanistic studies, and manipulation of the catalytic properties such as substrate specificity to generate novel catalysts.
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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