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Docking and electron transfer reactions of metalloproteins studied using site-directed mutants of cytochrome c

Reference	C17977
Principal Investigator / Supervisor	Professor Mike Wilson
Co-Investigators / Co-Supervisors	Professor Peter Nicholls, Professor Christopher Reynolds, Prof. Glyn Stanway
Institution	University of Essex
Department	Biological Sciences
Funding type	Research
Value (£)	199,052
Status	Completed
Type	Research Grant
Start date	01/12/2002
End date	01/12/2005
Duration	36 months

Abstract

Existing mutants of yeast iso-1 cytochrome c, in which the intrinsic methionine ligand to the iron is replaced by a non-binding residue, will be further engineered to form a cavity/channel near the haem so that the quantum yield for CO photodissociation is high (more than 3). These mutants will have the capacity to deliver electrons rapidly to redox partners on laser photolysis of the CO complex. The ligand binding and redox properties will be determined and the dynamics of the switch of the intrinsic ligand on change in pH or redox state is investigated. The binding properties of the selected mutants to redox partners will be determined and the ability to deliver electrons on photolysis screened using a range of protein electron acceptors. Electron transfer to cytochrome c oxidase catalytic intermediates will be studied as will docking using surface mutations of the engineered cytochrome c and COX subunit II.

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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