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Quantum catalysis in enzymes - beyond the transition state theory paradigm

ReferenceB19724/2
Principal Investigator / Supervisor Professor Nigel Scrutton
Co-Investigators /
Co-Supervisors
Professor David Leys, Professor Michael Sutcliffe
Institution The University of Manchester
DepartmentLife Sciences
Funding typeResearch
Value (£) 169,002
StatusCompleted
TypeResearch Grant
Start date 01/09/2005
End date 31/05/2007
Duration21 months

Abstract

Quantum tunnelling is now established as an important mechanism in enzyme catalysis. Using an unparalleled paradigm system, aromatic amine dehydrogenase (AADH), we will investigate systematically the importance of energy barrier shape - rather than simply height as with transition state theory - in controlling reaction rate. We will probe factors in both the enzyme and substrate that affect the shape of the barrier and protein motion using: time-resolved crystallography, studies of tunnelling rates and kinetic isotope effects in wild-type and mutant AADH, a series of modified substrates with perturbed tunnelling characteristics and computational chemistry. Our work will provide crucial new mechanistic insights into C - H bond cleavage by enzymes.

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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