Detection of Sulfide Release from the Oxygen-sensing [4Fe-4S] Cluster of FNR

Crack, Jason C., Green, Jeffrey, Le Brun, Nick E. and Thomson, Andrew J. (2006) Detection of Sulfide Release from the Oxygen-sensing [4Fe-4S] Cluster of FNR. Journal of Biological Chemistry, 281 (28). pp. 18909-18913. ISSN 0021-9258

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Abstract

The Escherichia coli FNR protein regulates the transcription of >100 genes in response to environmental O2, thereby coordinating the response to anoxia. Under O2-limiting conditions, FNR binds a [4Fe-4S]2+ cluster through four cysteine residues (Cys20, Cys23, Cys29, Cys122). The acquisition of the [4Fe-4S]2+ cluster converts FNR into the transcriptionally active dimeric form. Upon exposure to O2, the cluster converts to a [2Fe-2S]2+ form, generating FNR monomers that no longer bind DNA with high affinity. The mechanism of the cluster conversion reaction and the nature of the released iron and sulfur are of considerable current interest. Here, we report the application of a novel in vitro method, involving 5,5′-dithiobis-(2-nitrobenzoic acid), for determining the oxidation state of the sulfur atoms released during FNR cluster conversion following the addition of O2. Conversion of [4Fe-4S]2+ to [2Fe-2S] 2+ clusters by O2 for both native and reconstituted FNR results in the release of ∼2 sulfide ions per [4Fe-4S]2+ cluster. This demonstrates that the reaction between O2 and the [4Fe-4S] 2+ cluster does not require sulfide oxidation and hence must entail iron oxidation.

Item Type:	Article
Uncontrolled Keywords:	biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	18 Jun 2025 08:30
Last Modified:	18 Jun 2025 08:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/99592
DOI:	10.1074/jbc.C600042200

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