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

ReferenceC19031
Principal Investigator / Supervisor Professor Nigel Scrutton
Co-Investigators /
Co-Supervisors
Professor David Leys, Professor Andrew Munro, Professor Michael Sutcliffe
Institution University of Leicester
DepartmentBiochemistry
Funding typeResearch
Value (£) 190,784
StatusCompleted
TypeResearch Grant
Start date 01/06/2003
End date 31/08/2005
Duration27 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 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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