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Stopped-flow infra-red spectroscopy of metallo- proteins of environmental and commercial importance
Reference
BBS/E/J/00004124
Principal Investigator / Supervisor
Professor R Thorneley
Co-Investigators /
Co-Supervisors
Institution
John Innes Centre
Department
John Innes Centre Department
Funding type
Research
Value (£)
56,867
Status
Completed
Type
Institute Project
Start date
01/04/1997
End date
31/12/1998
Duration
21 months
Abstract
High resolution stopped-flow infra-red spectroscopy has been recently developed. The technique has clear potential for the determination of the mechanism of small molecule activation by metallo- proteins. The 1800-2200 cm-1 region, clear of protein and solvent bands, will be used to monitor directly enzyme bound intermediates in N2, N3, CN, C2H2 reduction (and CO inhibition) on native and recombinant variants of nitrogenase. Model systems will provide novel chemistry to calibrate and optimise the equipment. Cu- dissimilatory nitrite reductase (NO+N2O formation) and various peroxidases of commercial interest will also be investigated.
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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