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Relationship between novel structural features and function in cytochrome cd1 nitrite reductase
Reference
B05860
Principal Investigator / Supervisor
Professor Stuart John Ferguson
Co-Investigators /
Co-Supervisors
Institution
University of Oxford
Department
Biochemistry
Funding type
Research
Value (£)
162,352
Status
Completed
Type
Research Grant
Start date
20/09/1996
End date
20/05/2000
Duration
44 months
Abstract
The crystal structure of cytochrome cd1 (nitrite reductase) shows that the polypeptide has two domains, one containing the c-haem and the other the d1-haem. We will: (i) test mechanistic proposals made on the basis of the structure; and (ii) investigate the basis for the extensive conformational change and haem-iron ligand exchange that occurs in the c-haem domain upon its reduction. Variants of cytochrome cd1 carrying site-directed mutations will be obtained and characterised by crystallography and kinetic analysis of NO2-reductase and oxidase activities. Independent expression of the c-haem domain will determine whether redox changes at the c-haem centre are the determinant for the structural change.
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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