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Structure and function of the quinone binding site of the photosystem 1 reaction centre
Reference
C07809
Principal Investigator / Supervisor
Professor M Evans
Co-Investigators /
Co-Supervisors
Professor Peter Heathcote
,
Dr Stephen Rigby
Institution
University College London
Department
Genetics Evolution and Environment
Funding type
Research
Value (£)
193,394
Status
Completed
Type
Research Grant
Start date
01/09/1997
End date
01/12/2000
Duration
39 months
Abstract
Photosystem 1 provides the low potential reductant for autotrophic growth. The photochemical generation of this reductant with high quantum efficiency involves a electron acceptor chain bound to PSI polypeptides including phylloquinone. The redox potential of this quinone is altered by - 700mV by the protein environment. A range of spectroscopic techniques together with isotopic substitution of the quinone or of animo acids will be used to determine the properties of the quinone binding site. Site directed mutants will provide modified quinone binding, allowing the programme to identify critical factors in the protein environment functioning in the control of the redox and kinetic properties of this quinone. Understanding the mechanism of redox control by this site will be a major contribution to our knowledge of regulation of electron transfer in complex multicentre enzyme systems.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
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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