Award details

Quantum catalysis in enzymes - beyond the transition state theory paradigm

Reference	B19724
Principal Investigator / Supervisor	Professor Nigel Scrutton
Co-Investigators / Co-Supervisors	Professor David Leys, Professor Michael Sutcliffe
Institution	University of Leicester
Department	Biochemistry
Funding type	Research
Value (£)	383,354
Status	Completed
Type	Research Grant
Start date	01/02/2004
End date	31/08/2005
Duration	19 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 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

Associated awards:

B19724/2 Quantum catalysis in enzymes - beyond the transition state theory paradigm

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