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Acquisition of the cytochrome c fold
Reference
B19947
Principal Investigator / Supervisor
Professor Stuart John Ferguson
Co-Investigators /
Co-Supervisors
Professor Christina Redfield
,
Professor Lorna Smith
Institution
University of Oxford
Department
Biochemistry
Funding type
Research
Value (£)
207,438
Status
Completed
Type
Research Grant
Start date
01/11/2003
End date
31/03/2007
Duration
41 months
Abstract
The cytochrome c fold as exemplified by mitochondrial cytochrome c occurs in most organisms. The apo protein has long been regarded as largely unstructured and thus the formation of two thioether bonds between the heme and cysteine thiols of a CXXCH motif has been seen as critical for acquisition of the tertiary structure. Using newly developed systems, including an AXXAH variant protein, we have shown that the apo forms of both mitochondrial and thermophilic c-type cytochrome have considerably more structure than previously thought. We shall use NMR and mass spectrometry to elucidate these previously unsuspected structural features and why the thioether bonds are normally needed for the cytochrome c fold.
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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