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Conformational changes in proton-translocating transhydrogenases from mammalian mitochondria and bacteria

Reference	C14339
Principal Investigator / Supervisor	Professor Baz Jackson
Co-Investigators / Co-Supervisors	Dr Scott Andrew White
Institution	University of Birmingham
Department	Sch of Biosciences
Funding type	Research
Value (£)	187,940
Status	Completed
Type	Research Grant
Start date	08/05/2001
End date	08/05/2004
Duration	36 months

Abstract

The objective is to characterise conformational changes in transhydrogenase that are responsible for gating, (a) between states in which the chemical reaction (hydride transfer) is either allowed or forbidden, and (b) between states in which proton access is towards either the 'inside' or the 'outside' of the membrane. To ensure efficient coupling between a chemical reaction and an ion-electrochemical gradient, equivalent gating is essential to the operation of all conformationally-coupled pumps, but is generally very poorly understood. Analysis of these fundamental processes in transhydrogenase is made possible by recent technical developments, and by advances in our understanding of the enzyme structure.

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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