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Paracoccus pantotrophus cytochrome cd1 nitrite reductase; correlating novel structures with new kinetic insights
Reference
B11988
Principal Investigator / Supervisor
Professor Stuart John Ferguson
Co-Investigators /
Co-Supervisors
Professor Robert Conlan
,
Dr Nicholas James Watmough
Institution
University of Oxford
Department
Biochemistry
Funding type
Research
Value (£)
179,901
Status
Completed
Type
Research Grant
Start date
10/01/2000
End date
10/01/2003
Duration
36 months
Abstract
Paracoccus pantotrophus cytochrome cd1 undergoes a remarkable structural change upon reduction. The c-type cytochrome heme centre exchanges a histidine for a methionine and the d1 heme loses a tyrosine so as to open the active site. The relation of this structural change to the catalytic mechanism of the protein will be sought by a variety of spectroscopic and kinetic methods, afforded appropriately by use of mutants. In particular, this study will employ the new technique of stopped flow FTIR spectroscopy in collaboration with the John Innes Centre. Three catalytic activities of the enzyme will be studied; one e reduction of nitrite to nitric oxide, two e reduction of hydroxylamine to ammonia and four e reduction of oxygen to water.
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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