Award details

The coupling of ATP hydrolysis to metal insertion in magnesium chelatase

Reference	C15593
Principal Investigator / Supervisor	Krebs Professor of B Christopher Hunter
Co-Investigators / Co-Supervisors	Dr Jim Reid
Institution	University of Sheffield
Department	Molecular Biology and Biotechnology
Funding type	Research
Value (£)	243,204
Status	Completed
Type	Research Grant
Start date	01/11/2001
End date	01/11/2004
Duration	36 months

Abstract

Magnesium chelatase lies at the branchpoint in tetrapyrrole in biosynthesis, and catalyses the insertion of magnesium into protoporphyrin, the first committed step in chlorophyll biosynthesis. It consists of three subunits which combine to couple free energy of ATP hydrolysis of Mg2+ into porphyrin. We will: 1. Use transient kinetic methods to characterise the binding and hydrolysis of ATP and phosphate release. 2. Follow the insertion of Mg2+ into enzyme-bound porphyrin using stopped-flow kinetic methods, by monitoring fluorescence of porphyrin and protein. 3. Conduct crystallisation trials on the chelatase, as well as using single particle analysis to obtain information at low resolution on the arrangement of subunits within the complex.

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

I accept the terms and conditions of use (opens in new window)

export PDF file

back to list new search