Award details

Nitrite reduction by paracoccus pantotrophus cytochrome cd1; structural mobility and mechanism of a NO generating enzyme

Reference	C19430
Principal Investigator / Supervisor	Professor Stuart John Ferguson
Co-Investigators / Co-Supervisors	Professor Robert Conlan
Institution	University of Oxford
Department	Biochemistry
Funding type	Research
Value (£)	204,624
Status	Completed
Type	Research Grant
Start date	10/05/2003
End date	09/05/2006
Duration	36 months

Abstract

The aim of this programme is to elucidate the detailed mechanism of the physiological nitrite reductase reaction of this enzyme. In particular we wish to understand how the release of the product, nitric oxide, is controlled by the specialised d1 heme active site, rather than being trapped here as a stable ferrous heme-nitric oxide adduct. The proposed work will draw upon new knowledge of conformations that can be adopted by cytochrome cd1 as well as considerably extend our analysis of the nitrite reductase reaction. In order to do this we need to deploy a wide range of methods, including mutagenesis, x-ray crystallography and a number of different, but complementary time-resolved spectroscopies. (Joint with grant number 19434).

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:

C19434 Nitrite reduction by Paracoccus pantotrophus cytochrome cd1: structural mobility and mechanism of a NO generating enzyme

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