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Acquisition of the cytochrome c fold

ReferenceB19947
Principal Investigator / Supervisor Professor Stuart John Ferguson
Co-Investigators /
Co-Supervisors
Professor Christina Redfield, Professor Lorna Smith
Institution University of Oxford
DepartmentBiochemistry
Funding typeResearch
Value (£) 207,438
StatusCompleted
TypeResearch Grant
Start date 01/11/2003
End date 31/03/2007
Duration41 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 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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