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X-ray structure of the catalytic component of benzene dioxygenase

ReferenceBCI06226
Principal Investigator / Supervisor Professor Brian Sutton
Co-Investigators /
Co-Supervisors
Professor Jeremy Richard Mason
Institution King's College London
DepartmentGKT School of Biomedical Sciences
Funding typeResearch
Value (£) 184,976
StatusCompleted
TypeResearch Grant
Start date 01/09/1996
End date 01/09/1999
Duration36 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative Biological Chemistry Initiative (BCI) [1995]
Funding SchemeX – not Funded via a specific Funding Scheme
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