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An integrated approach to define the mechanism of respiratory nitrate reduction: spectroscopic and voltammetric studies

ReferenceB17233
Principal Investigator / Supervisor Professor Julea Butt
Co-Investigators /
Co-Supervisors
Professor David Richardson
Institution University of East Anglia
DepartmentChemistry
Funding typeResearch
Value (£) 181,928
StatusCompleted
TypeResearch Grant
Start date 29/07/2002
End date 28/02/2006
Duration43 months

Abstract

The molybdoprotein NarGHI is essential for the respiratory flexibility of many denitrifying, enteric and pathogenic bacteria. We have demonstrated that the nitrate reducing dimer, NarGH, catalyses nitrate reduction through two kinetically distinct pathways. These pathways are reversibly interconverted by a redox switch within the enzyme which may be provided by oxidation state changes of the molybdenum or [Fe-S] clusters within the enzyme. We now propose to distinguish between these possibilities and elucidate the mechanism of respiratory nitrate reduction at a molecular level through a combination of spectroscopic and voltammetric methodologies together with scanning probe microscopies.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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