Reactions of nitric oxide and oxygen with the regulator of fumarate and nitrate reduction, a global transcriptional regulator, during anaerobic growth of Escherichia coli

Crack, Jason C., Le Brun, Nick E., Thomson, Andrew J., Green, Jeffrey and Jervis, Adrian J. (2008) Reactions of nitric oxide and oxygen with the regulator of fumarate and nitrate reduction, a global transcriptional regulator, during anaerobic growth of Escherichia coli. Methods in Enzymology, 437. pp. 191-209. ISSN 1557-7988

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Abstract

The Escherichia coli fumarate and nitrate reductase (FNR) regulator protein is an important transcriptional regulator that controls the expression of a large regulon of more than 100 genes in response to changes in oxygen availability. FNR is active when it acquires a [4Fe-4S]2+ cluster under anaerobic conditions. The presence of the [4Fe-4S]2+ cluster promotes protein dimerization and site-specific DNA binding, facilitating activation or repression of target promoters. Oxygen is sensed by the controlled disassembly of the [4Fe-4S]2+ cluster, ultimately resulting in inactive, monomeric, apo-FNR. The FNR [4Fe-4S]2+ cluster is also sensitive to nitric oxide, such that under anaerobic conditions the protein is inactivated by nitrosylation of the iron-sulfur cluster, yielding a mixture of monomeric and dimeric dinitrosyl-iron cysteine species. This chapter describes some of the methods used to produce active [4Fe-4S] FNR protein and investigates the reaction of the [4Fe-4S]2+ cluster with nitric oxide and oxygen in vitro.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes
Depositing User:	Rachel Smith
Date Deposited:	07 Apr 2011 14:11
Last Modified:	06 Feb 2025 02:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/28490
DOI:	10.1016/S0076-6879(07)37011-0

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