Award details

Mechanisms of Proton Transfer to Nitrogenase Substrates

Reference	BBS/E/J/40004039
Principal Investigator / Supervisor	Dr Richard Henderson
Co-Investigators / Co-Supervisors	Dr David Hughes
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	265,847
Status	Completed
Type	Institute Project
Start date	01/04/1997
End date	31/03/2001
Duration	48 months

Abstract

The nitrogenases convert dinitrogen to ammonia by a sequence of electron- and proton-transfer reactions. In addition a variety of other small molecules can be transformed in a similar fashion in vitro. This project defines the mechanistic roles played by protons in all aspects of the enzymic transformation of the substrates: binding; conversion to products and product release, and complements RO 4035. Studies typically involve the synthesis and X-ray crystallographic structural characterisation of new mononuclear and binuclear complexes (complements RO 4050) which are capable of binding the nitrogenase substrates. The protonation reactions of these complexes are then studied using rapid reaction techniques. Thus chemical precedent gives mechanistic insight into enzymatic pathways

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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