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Stopped-flow infra-red spectroscopy of metalloproteins of environmental and commercial importance

Reference	MOL04637
Principal Investigator / Supervisor	Professor R Thorneley
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	Disease and Stress Biology
Funding type	Research
Value (£)	151,622
Status	Completed
Type	Research Grant
Start date	01/01/1996
End date	01/01/1999
Duration	36 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 Fe/Co-nitrile hydratase (commercial chiral and bulk amide synthesis) 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	Molecules (Ropa) (MOL) [1994]
Funding Scheme	X – not Funded via a specific Funding Scheme

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