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Molybdate update, processing and sensing

Reference	BBS/E/J/40004025
Principal Investigator / Supervisor	Professor David Lawson
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	291,461
Status	Completed
Type	Institute Project
Start date	01/04/1997
End date	30/09/2000
Duration	42 months

Abstract

Mo is the only metal in the second transition series that is crucial for life. It occurs in cofactors of redox enzymes that catalyse reactions at C, S and N atoms, including nitrate reductase and nitrogenase which play a vital role in the nitrogen cycle. A key question in studying proteins containing Mo is to understand the intrinsic interactions that contribute to its biological role. The project focuses on the molecular interactions in three major integrated processes involving Mo: transport, processing, and sensing. Mo is found in the environment as molybdate. Cells distinguish between molybdate and other chemically similar inorganic oxyanions, e.g. sulphate, and phosphate. Bacterial periplasmic and cytoplasmic Mo-binding proteins involved in transport, processing and homeostasis provide models for determining how cells differentially take up and distribute this essential trace element. The Mo- dependent repressor is a new class of regulatory protein that couples metal binding with transcriptional regulation

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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