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Protein-protein and substrate protein interactions in magnesium chelatase

Reference	C10281
Principal Investigator / Supervisor	Krebs Professor of B Christopher Hunter
Co-Investigators / Co-Supervisors
Institution	University of Sheffield
Department	Molecular Biology and Biotechnology
Funding type	Research
Value (£)	173,337
Status	Completed
Type	Research Grant
Start date	02/11/1998
End date	02/11/2001
Duration	36 months

Abstract

Magnesium chelatase lies at the branchpoint in tetrapyrrole biosynthesis, and catalyses the insertion of magnesium into protoporphyrin. It consists of three subunits, H, I and D, which can be overproduced in E. coli, and combined in vitro to form an active, ATP-driven enzyme. A detailed investigation of this enzyme is proposed, using a variety of spectroscopic, steady- state and pre-steady-state techniques. The objectives are to characterise: (i) the interaction between the H subunit and protoporphyrin, (ii) the interaction of I with D, and (iii) the role of ATP hydrolysis in the chelation reaction.

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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