Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/45531
Title: Dioxygen controls the nitrosylation reactions of a protein-bound [4Fe4S] cluster
Authors: Grabarczyk, Daniel B.
Ash, Philip A.
Myers, William K.
Dodd, Erin L.
Vincent, Kylie A.
First Published: 9-Sep-2019
Publisher: Royal Society of Chemistry
Citation: Dalton Transactions, 2019
Abstract: Iron–sulfur clusters are exceptionally tuneable protein cofactors, and as one of their many roles they are involved in biological responses to nitrosative stress. Both iron–sulfur proteins and synthetic model clusters are extremely sensitive to nitrosylation, tending towards rapid multi-step reaction and cluster degradation. Reaction of protein-bound iron–sulfur clusters with nitric oxide can be stopped at partial nitrosylation in vivo, and repair of protein-bound nitrosylated clusters is possible in the cellular environment. We have used a combination of infrared, EPR, and UV-visible spectroscopies to show that a model [4Fe4S] cluster-containing protein, A. ferroxidans high potential iron–sulfur protein (HiPIP), reacts with NO to give a product mixture dominated by Roussin's Black Salt (RBS) and Roussin's Red Ester (RRE) species. We have shown that O2 plays a critical role in controlling the major product of nitrosylation, with RBS-like products favoured under strictly anaerobic conditions and RRE favoured in the presence of trace O2. Moreover, addition of trace O2 to anaerobically nitrosylated samples induces conversion of RBS-like products to RRE. These findings may have implications for mechanisms of iron–sulfur cluster repair following nitrosative stress, suggest a crucial role for trace O2, and provide an important link between nitrosylation chemistry of iron–sulfur proteins and the well-established reactivity of synthetic iron–sulfur clusters.
DOI Link: 10.1039/C9DT00924H
ISSN: 1477-9226
Links: https://pubs.rsc.org/en/content/articlelanding/2019/DT/C9DT00924H#!divAbstract
http://hdl.handle.net/2381/45531
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2019. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description: Electronic supplementary information (ESI) available. See DOI: 10.1039/c9dt00924h
Appears in Collections:Published Articles, Dept. of Chemistry

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