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Redox-linked structural changes in the activation of bacterial di-heme cytochrome c peroxidases

ReferenceB10987
Principal Investigator / Supervisor Dr Nicholas James Watmough
Co-Investigators /
Co-Supervisors
Professor Robert Conlan
Institution University of East Anglia
DepartmentBiological Sciences
Funding typeResearch
Value (£) 192,868
StatusCompleted
TypeResearch Grant
Start date 15/02/1999
End date 29/11/2002
Duration45 months

Abstract

The X-ray structure at 2.4 Angstrom of the resting state of di-heme cytochrome c peroxidase (CCP) from Pseudomonas aeruginosa shows both hemes to be six-coordinate and unable to bind substrate. Reduction of high-potential heme in the C-terminal domain induces structural changes in the protein that lead to the loss of a protein axial ligand from one of the hemes to form the substrate binding site. This programme aims to explore these structural changes using a combination of protein-engineering, X-ray crystallography, 19F-NMR and rapid reaction kinetics. The structure of the activated (half reduced) CCP will be used as a basis to elucidate the role of a novel calcium binding site identified in the X-ray structure and to obtain a detailed description of the reaction mechanism of this enzyme.

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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