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Alternative Nitrogenases
Reference
BBS/E/J/40004032
Principal Investigator / Supervisor
Dr Robert Eady
Co-Investigators /
Co-Supervisors
Professor David John Lowe
Institution
John Innes Centre
Department
John Innes Centre Department
Funding type
Research
Value (£)
277,383
Status
Completed
Type
Institute Project
Start date
01/04/1997
End date
31/03/2001
Duration
48 months
Abstract
The discovery of alternative nitrogenase systems which do not utilise molybdenum fundamentally changed the view of the chemistry of biological N2 reduction which, until 1985, had held that Mo was essential for catalysis. These enzymes are genetically distinct but comparison of the amino acid sequences of Mo- nitrogenases with those of the V-nitrogenases of A. vinelandii and A. chroococcum, and the Fe-Nitrogenase of A. vinelandii shows that the residues which bind FeMoco and `P' clusters in the x-ray structure of Mo-nitrogenase are conserved in all three nitrogenases. The alternative nitrogenases utilise different metals in cofactor centres homologous to FeMoco the catalytic centre of Mo-nitrogenase. These differences are being exploited in an interdisciplinary study involving genetics, biochemistry and physiology which aims to elucidate how metal substitution affects reactivity of nitrogenase towards N2 (cf. RO 4035). In addition, this study contributes to an understanding of how environmental factors, such as metal availability, temperature and the dioxygen concentration affect the microbial physiology of diazotrophic growth. Over the past four years biochemical research on Mo- independent nitrogenases has stimulated new areas of work on the synthesis and reactivity of V and Fe chemical systems capable of binding and transforming N2 (RO 4050)
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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