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Chemistry and function of the active site of P450 BM3 probed by resonance Raman and surface enhanced resonance Raman scattering
Reference
B12703
Principal Investigator / Supervisor
Professor William Smith
Co-Investigators /
Co-Supervisors
Professor Andrew Munro
Institution
University of Strathclyde
Department
Pure and Applied Chemistry
Funding type
Research
Value (£)
217,136
Status
Completed
Type
Research Grant
Start date
01/07/2000
End date
15/08/2003
Duration
37 months
Abstract
Cytochrome P450 BM3 is the best understood soluble P450 and is an ideal system to advance understanding of P450 mechanism. New developments in resonance Raman and surface enhanced resonance Raman scattering and the informative nature of the selective scattering from haem and flavin chromophores, combined with the availability of key mutants will be used to define in situ active site structure and catalytic intermediates, and to understand interactions between P450 and other proteins, and consequently P450 function. Specific targets to be characterised are: (1) active site structure in wild-type/mutant P450s, (2) substrate-, ligand- and cofactor-dependent effects on P450 BM3 haem & flavin signals, (3) inter-protein effects, including domain/domain and P450/cytochrome b5 interactions, and (4) properties of the oxygen complexes of P450 BM3, using freeze-quenching to trap short-lived intermediates.
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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