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X-ray studies of nitrite reductase rusticyanin and their site specific mutants
Reference
B14224
Principal Investigator / Supervisor
Professor Samar Hasnain
Co-Investigators /
Co-Supervisors
Institution
STFC - Laboratories
Department
Photon Science
Funding type
Research
Value (£)
267,596
Status
Completed
Type
Research Grant
Start date
02/01/2001
End date
01/07/2004
Duration
42 months
Abstract
Cupredoxin fold is widely found in multicopper proteins such as nitrite reductases and oxidases including ceruloplasmin and ascorbate oxidase. Rusticyanin is the most stable of the cupredoxin family with a very high redox potential. We have determined X-ray structures of both Rusticyanin and blue copper nitrite reductase and have made major progress with the molecular biology of both. We propose to build on these and to design a number of mutants and determine their structures to address questions such as: (i) the structural features which makes the Rusticyanin so acid stable and possess the highest redox potential of the cupredoxins. (ii) the proton abstraction mechanism is operative in nitrite reductase and that the two substrates are gated via the two links between the two copper sites. In addition, we have noted that the catalytic copper site in nitrite reductase is highly specific to the Cu metal and have suggested that its incorporation may require a specific chaperone in much the same way as is believed to be the case for cytochrome c oxidase and superoxide dismutase. A systematic search for the nitrite reductase's chaperone is being pursued and we will undertake its structural studies as well as its complex with NiR.
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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