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Primary events in an ion pump: active site rearrangements during the redox reaction of transhydrogenase.

Reference	BBS/B/01456
Principal Investigator / Supervisor	Professor Baz Jackson
Co-Investigators / Co-Supervisors	Professor Timothy Dafforn, Dr John Snaith, Dr Scott Andrew White
Institution	University of Birmingham
Department	Sch of Biosciences
Funding type	Research
Value (£)	222,610
Status	Completed
Type	Research Grant
Start date	01/10/2004
End date	30/09/2007
Duration	36 months

Abstract

Using combinations of bound tetra-hydro analogues of NADH and NADPH and physiological nucleotides, we will solve X-ray structures equivalent to the ground state for hydride transfer in wild-type and selected mutants of transhydrogenase. These studies will indicate how nucleotides are polarised during the redox reaction and how local events lead to the propagation of conformational changes, including the closure of the cleft between the to NADH-binding domains, that are linked to proton translocation by the enzyme. The importance of the structural rigidity of the peripheral NADH-binding domain to the coupling between active-site events and cleft closure will be investigated in studies in which the fluorescence and phosphorescence emissions of the sole tryptophan residue are correlated with measurements of nucleotide binding and hydride transfer.

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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