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Structural basis of nitric oxide reduction and regulation thereof in Paracoccus denitrificans
Reference
B19851
Principal Investigator / Supervisor
Professor David Richardson
Co-Investigators /
Co-Supervisors
Institution
University of East Anglia
Department
Biological Sciences
Funding type
Research
Value (£)
194,887
Status
Completed
Type
Research Grant
Start date
01/02/2004
End date
31/05/2007
Duration
40 months
Abstract
Bacterial nitric oxide reductase (NOR) is an integral membrane protein that catalyses the reduction of nitric oxide in a crucial step of denitrification or as a means of neutralising the nitric oxide that is released by macrophages as part of the human immune response. It is a distinct member of the superfamily of haem/copper oxidases. We will determine a structure of a soluble domain of the NOR from Paracoccus denitrificans, improve crystals of membrane-bound NOR to facilitate a structure determination, and conduct molecular studies on the regulatory proteins NorQ and NorD. These studies will provide detailed information on the mechanisms of NO reduction, proton and electron transport in NOR, and post-translational regulation by NorQD.
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
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