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Issue 47, 2018
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Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe–4S] NsrR

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Abstract

The bacterial nitric oxide (NO)-sensing transcriptional regulator NsrR binds a [4Fe–4S] cluster that enables DNA-binding and thus repression of the cell's NO stress response. Upon exposure to NO, the cluster undergoes a complex nitrosylation reaction resulting in a mixture of iron-nitrosyl species, which spectroscopic studies have indicated are similar to well characterized low molecular weight dinitrosyl iron complex (DNIC), Roussin's Red Ester (RRE) and Roussin's Black Salt (RBS). Here we report mass spectrometric studies that enable the unambiguous identification of NsrR-bound RRE-type species, including a persulfide bound form that results from the oxidation of cluster sulfide. In the presence of the low molecular weight thiols glutathione and mycothiol, glutathionylated and mycothiolated forms of NsrR were readily formed.

Graphical abstract: Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe–4S] NsrR

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Supplementary files

Article information


Submitted
15 Feb 2018
Accepted
04 Apr 2018
First published
23 May 2018

This article is Open Access

Chem. Commun., 2018,54, 5992-5995
Article type
Communication

Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe–4S] NsrR

J. C. Crack, C. J. Hamilton and N. E. Le Brun, Chem. Commun., 2018, 54, 5992
DOI: 10.1039/C8CC01339J

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