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

Crack, Jason C., Hamilton, Chris J. and Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061 (2018) Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe-4S] NsrR. Chemical Communications, 54 (47). pp. 5992-5995. ISSN 1359-7345

Preview

PDF (Crack_etal_ChemComm_2018) - Published Version Available under License Creative Commons Attribution. Download (2MB) | Preview

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.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry Faculty of Science > School of Pharmacy
UEA Research Groups:	Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemical Biology and Medicinal Chemistry (former - to 2021) Faculty of Science > Research Groups > Chemistry of Life Processes
Depositing User:	Pure Connector
Date Deposited:	19 Apr 2018 10:36
Last Modified:	21 Oct 2022 18:36
URI:	https://ueaeprints.uea.ac.uk/id/eprint/66809
DOI:	10.1039/c8cc01339j

Actions (login required)

View Item