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Structures of short-lived physiological electron transfer complexes

ReferenceB18118/2
Principal Investigator / Supervisor Professor David Leys
Co-Investigators /
Co-Supervisors
Professor Nigel Scrutton, Professor Michael Sutcliffe
Institution The University of Manchester
DepartmentLife Sciences
Funding typeResearch
Value (£) 27,751
StatusCompleted
TypeResearch Grant
Start date 01/02/2006
End date 31/07/2006
Duration6 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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