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Structures of short-lived physiological electron transfer complexes
Reference
B18118
Principal Investigator / Supervisor
Professor David Leys
Co-Investigators /
Co-Supervisors
Professor Nigel Scrutton
,
Professor Michael Sutcliffe
Institution
University of Leicester
Department
Biological NMR Centre
Funding type
Research
Value (£)
163,852
Status
Completed
Type
Research Grant
Start date
01/03/2003
End date
31/08/2005
Duration
30 months
Abstract
Weakly associated physiological electron transfer (eT) complexes have remained elusive to structural studies. Our work targets understanding of the structural elements of complex formation between redox proteins that undergo large-scale conformational change as a prerequisite to complex assembly, using the ETF proteins as paradigm model systems. The ETFs are highly mobile proteins that interact with a number of key primary dehydrogenases, complexes for which we seek high-resolution structures. Our work will provide atomic insight into a new robust engineering principle for interprotein electron transfer, allowing for specific recognition of multiple redox partners, whilst maintaining efficient electron transfer rates. This will have general implications for physiological, protein-mediated electron transfer.
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
Associated awards:
B18118/2 Structures of short-lived physiological electron transfer complexes
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