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. ORCID: https://orcid.org/0000-0001-9780-4061, 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:	24 Sep 2024 09:31
URI:	https://ueaeprints.uea.ac.uk/id/eprint/28490
DOI:	10.1016/S0076-6879(07)37011-0

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