Nitrosylation of nitric-oxide-sensing regulatory proteins containing [4Fe-4S] clusters gives rise to multiple iron-nitrosyl complexes

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Serrano, Pauline N., Wang, Hongxin, Crack, Jason C., Prior, Christopher, Hutchings, Matthew I., Thomson, Andrew J., Kamali, Saeed, Yoda, Yoshitaka, Zhao, Jiyong, Hu, Michael Y., Alp, Ercan E., Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146, Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061 and Cramer, Stephen P. (2016) Nitrosylation of nitric-oxide-sensing regulatory proteins containing [4Fe-4S] clusters gives rise to multiple iron-nitrosyl complexes. Angewandte Chemie International Edition, 55 (47). 14575–14579. ISSN 1433-7851

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Abstract

The reaction of protein-bound iron–sulfur (Fe-S) clusters with nitric oxide (NO) plays key roles in NO-mediated toxicity and signaling. Elucidation of the mechanism of the reaction of NO with DNA regulatory proteins that contain Fe-S clusters has been hampered by a lack of information about the nature of the iron-nitrosyl products formed. Herein, we report nuclear resonance vibrational spectroscopy (NRVS) and density functional theory (DFT) calculations that identify NO reaction products in WhiD and NsrR, regulatory proteins that use a [4Fe-4S] cluster to sense NO. This work reveals that nitrosylation yields multiple products structurally related to Roussin's Red Ester (RRE, [Fe2(NO)4(Cys)2]) and Roussin's Black Salt (RBS, [Fe4(NO)7S3]. In the latter case, the absence of 32S/34S shifts in the Fe−S region of the NRVS spectra suggest that a new species, Roussin's Black Ester (RBE), may be formed, in which one or more of the sulfide ligands is replaced by Cys thiolates.

Item Type: Article
Uncontrolled Keywords: gene regulation,iron–sulfur clusters,nitric oxide,nuclear vibrational resonance spectroscopy,synchrotron radiation
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Science
Faculty of Science > School of Biological Sciences
Depositing User: Pure Connector
Date Deposited: 11 Oct 2016 16:00
Last Modified: 09 Feb 2023 13:44
URI: https://ueaeprints.uea.ac.uk/id/eprint/60858
DOI: 10.1002/anie.201607033

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