Award details

Radical reappraisal of the mechanism of electron transfer and the role of calmodulin in nitric synthase

Reference	C18194
Principal Investigator / Supervisor	Professor Nigel Scrutton
Co-Investigators / Co-Supervisors	Professor Andrew Munro
Institution	University of Leicester
Department	Biochemistry
Funding type	Research
Value (£)	171,568
Status	Completed
Type	Research Grant
Start date	15/02/2003
End date	14/09/2005
Duration	31 months

Abstract

Calmodulin binding leads to accelerated electron transfer in nitric oxide synthase (NOS) and is the major control mechanism for (NOS) activity. Calmodulin also stimulates cytochrome c reduction by NOS reductase domain in steady-state assays, and has led USA and Japanese workers to propose a mechanism for calmodulin stimulated electron flow within the reductase domain. Our stopped-flow absorbance and fluorescence studies have indicated that these groups have misassigned a number of major kinetic phases, thus leading to inappropriate models for electron transfer. Based on our work, we have proposed a radically different mechanism and demonstrated no role for calmodulin in internal electron transfer in NOS reductase. We will validate and extend this new mechanism using advanced kinetic methods and resolve the controversies concerning regulation of NOS activity.

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
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

Associated awards:

C18194/2 Radical reappraisal of the mechanism of electron transfer and the role of calmodulin in nitric synthase

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