Award details

Conformational equilibria and electron transfer in NADPH-cytochrome P450 reductase

Reference	BBS/B/1311X
Principal Investigator / Supervisor	Professor Gordon Roberts
Co-Investigators / Co-Supervisors	Professor Andrew Munro, Professor Nigel Scrutton
Institution	University of Leicester
Department	Biochemistry
Funding type	Research
Value (£)	223,004
Status	Completed
Type	Research Grant
Start date	01/06/2004
End date	30/09/2007
Duration	40 months

Abstract

Cytochrome P450 reductase is an enzyme containing both FMN and FAD which donates electrons to cytochrome P450 which play pivotal roles in the oxidation of a wide spectrum of drugs and xenobiotics. It is related to a number of other diflavin reductases, including nitric oxide synthase and methionine synthase reductase. Evidence from our earlier work leads to the idea that domain movement plays an important role in the mechanism of the enzyme. We will use a combination of NMR, SAXS, stopped-flow and temperature-jump kinetics and mutagenesis to test this by relating structural and kinetic parameters in mutants designed to alter domain-domain interactions.

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

I accept the terms and conditions of use (opens in new window)

export PDF file

back to list new search