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Elucidating factors controlling enzymic H-tunnelling through structural and kinetic studies of dimethylglycine oxidase

Reference	C19031
Principal Investigator / Supervisor	Professor Nigel Scrutton
Co-Investigators / Co-Supervisors	Professor David Leys, Professor Andrew Munro, Professor Michael Sutcliffe
Institution	University of Leicester
Department	Biochemistry
Funding type	Research
Value (£)	190,784
Status	Completed
Type	Research Grant
Start date	01/06/2003
End date	31/08/2005
Duration	27 months

Abstract

We have provided the first example of enzyme catalysis by H- tunnelling from the substrate vibrational ground state driven by protein motion. This provides a new framework for catalysis, which applies to a number of redox enzymes and will have widespread importance in biological catalysis. We will elucidate the atomic structure of a novel flavoprotein oxidase that catalyses H-transfer by quantum tunnelling. We will study the H-tunnelling mechanism in wild-type and mutant forms to assess the role of compromising mutations on tunnelling regimes and thus address the role of barrier width, protein dynamics and tunnelling from vibrationally excited states, and provide important new information on folate's role in catalysis in this enzyme class.

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

Associated awards:

C19031/2 Elucidating factors controlling enzymic H-tunnelling through structural and kinetic studies of dimethylglycine oxidase

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