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Structure of molybdenum nitrogenase

Reference	BBS/E/J/00004026
Principal Investigator / Supervisor	Professor David Lawson
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	507,605
Status	Completed
Type	Institute Project
Start date	01/09/1997
End date	31/08/2000
Duration	36 months

Abstract

Molybdenum nitrogenase is the most widespread of the three enzymes responsible for biological Nitrogen Fixation. 3D X-ray crystallographic structures of both proteins of the enzyme from two species Asotobacter vinelandii and Clostridium pasteurianum have been published but differ in important detail. We have crystallised the molybdenum iron protein from Klebsiella pneumonia nitrogenase and have obtained X-ray crystallographic data at low temperature and higher resolution than that achieved by others. Analysis of these data has allowed resolution of these controversies. We are conducting a site- directed mutagenesis programme backed by spectroscopic and X- ray structural studies of the protein in a range of oxidation states to probe determinants of the structure and properties of the metallo-sulphur cluster prosthetic groups. This project is intimately related to RO4035 on mechanism of nitrogenase. The active site of the enzyme, the iron molybdenum cofactor FeMoco, is extracted from the protein on a large scale to allow chemical characterisation (see ROs 4040, 4050, 4055, 4056).

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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