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Assembly of respiratory hydrogenase complexes
Reference
P15018
Principal Investigator / Supervisor
Professor Frank Sargent
Co-Investigators /
Co-Supervisors
Institution
University of East Anglia
Department
Biological Sciences
Funding type
Research
Value (£)
183,440
Status
Completed
Type
Research Grant
Start date
01/11/2001
End date
31/10/2004
Duration
36 months
Abstract
Dihydrogen oxidation is an important feature of bacterial energy conservation and is catalysed by hydrogenase. The Escherichia coli hydrogenase-2 isoenzyme is a complex membrane-bounded nickel- dependent metalloenzyme. The ultimate event in the biosynthesis of the enzyme is the translocation of a fully folded core hydrogenase complex across the energy-transducing inner membrane. Transport is catalysed by the Tat apparatus; a system that has evolved for the transmembrane translocation of folded proteins. By studying synthesis of hydrogenase-2, the programme of research aims to identify chaperones required for hydrogenase signal peptide recognition/sequestration during assembly of this multi-subunit enzyme. The interrelationship between hydrogenase-2 and the Tat apparatus will be explored.
Summary
unavailable
Committee
Closed Committee - Plant & Microbial Sciences (PMS)
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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