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Molecular enzymology of FprA - a pivotal enzyme in M. tuberculosis redox chemistry

Reference	BBS/B/06288
Principal Investigator / Supervisor	Professor Andrew Munro
Co-Investigators / Co-Supervisors	Professor David Leys, Professor Nigel Scrutton
Institution	University of Leicester
Department	Biochemistry
Funding type	Research
Value (£)	207,930
Status	Completed
Type	Research Grant
Start date	01/06/2004
End date	31/08/2005
Duration	15 months

Abstract

Mycobacterium tuberculosis flavoprotein reductase A (FprA) is a central enzyme in mycobacterial physiology - which participates in electron transfer (eT) reactions to several P450s in the bacterium. It displays intriguing kinetic features typical of a bipartite mode of binding of NAD(P)H cofactors, an important regulatory phenomenon observed also in studies of nitric oxide synthase and cytochrome P450 reductase. The single flavin FprA is a tractable system for provision of a molecular description of this phenomenon, particularly given the ease with which FprA is crystallised and the quality of x-ray diffraction data obtainable. The aim of this study is to gain a fundamental knowledge of this regulatory phenomenon, combined with a detailed kinetic, structural and thermodynamic understanding of FprAs binding and eT reactions with cellular ferredoxin redox partners.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
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

Associated awards:

BBS/B/06288/2 Molecular enzymology of FprA - a pivotal enzyme in M. tuberculosis redox chemistry

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