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

Reference	B10987
Principal Investigator / Supervisor	Dr Nicholas James Watmough
Co-Investigators / Co-Supervisors	Professor Robert Conlan
Institution	University of East Anglia
Department	Biological Sciences
Funding type	Research
Value (£)	192,868
Status	Completed
Type	Research Grant
Start date	15/02/1999
End date	29/11/2002
Duration	45 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 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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