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Structure and function of nitric oxide reductase: an ancient oxidase

Reference	C10160
Principal Investigator / Supervisor	Professor Andrew Thomson
Co-Investigators / Co-Supervisors	Dr Myles Cheesman, Professor David Richardson, Dr S Spiro, Dr Nicholas James Watmough
Institution	University of East Anglia
Department	Chemistry
Funding type	Research
Value (£)	213,826
Status	Completed
Type	Research Grant
Start date	15/11/1998
End date	25/11/2002
Duration	48 months

Abstract

Nitric oxide reductase, the enzyme of bacterial denitrification which reduces NO to N2O, has a close structural homology with cytochrome c oxidase, CcO. Its contains a heme and non- heme-iron pair at the active site in contrast to the heme-copper centre for CcO. The programme will study the ligand binding properties of the dinuclear site to identify important catalytic intermediates and to compare its properties with those of the heme-copper site; it will elucidate intra- and inter-molecular electron transfers and measure bioenergetic properties including proton uptake, redox potentials and electrogenicity. Construction of site directed mutants will allow tests of enzyme mechanisms and help define the molecular architecture, especially of the catalytic site. Fundamental questions about the molecular basis of the evolution of proton pumps will be addressed.

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

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