ArticleFree radical biology & medicine2011
Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.
Article in Free radical biology & medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 55 citations in OpenAlex.
- Harnessing gasotransmitters for orthopaedic infection therapy: Mechanisms and advanced delivery platforms.Bioactive materials · 2027Review
- Research Progress of Nitrite Metabolism in Fermented Meat Products.Foods (Basel, Switzerland) · 2023Review
- Nitrites in Cured Meats, Health Risk Issues, Alternatives to Nitrites: A Review.Foods (Basel, Switzerland) · 2022Review
- Iron in leaves: chemical forms, signalling, and in-cell distribution.Journal of experimental botany · 2022Review
- Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and inhibits its electron transfer activity.Frontiers in molecular biosciences · 2022Article
- The Relationship of Glutathione-Molecules (Basel, Switzerland) · 2021Review
- Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism-Review.Molecules (Basel, Switzerland) · 2020Review
- Light-induced release of nitric oxide from the nitric oxide-bound CDGSH-type [2Fe-2S] clusters in mitochondrial protein Miner2.Nitric oxide : biology and chemistry · 2019Article
- Synthetic methodology for preparation of dinitrosyl iron complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Review
- EPR spectroscopy of complex biological iron-sulfur systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Binding of Nitric Oxide in CDGSH-type [2Fe-2S] Clusters of the Human Mitochondrial Protein Miner2.The Journal of biological chemistry · 2017Article
- Recent Advances in Multinuclear Metal Nitrosyl Complexes.Coordination chemistry reviews · 2016Article
- Breathing new life into nitric oxide signaling: A brief overview of the interplay between oxygen and nitric oxide.Redox biology · 2015Review
- The N-terminal domain of human DNA helicase Rtel1 contains a redox active iron-sulfur cluster.BioMed research international · 2014Article
- Catalase (KatA) plays a role in protection against anaerobic nitric oxide in Pseudomonas aeruginosa.PloS one · 2014Article
- A novel protein protects bacterial iron-dependent metabolism from nitric oxide.Journal of bacteriology · 2013Article
- Iron sulfur cluster proteins and microbial regulation: implications for understanding tuberculosis.Current opinion in chemical biology · 2012Review
- Hemoglobin: a nitric-oxide dioxygenase.Scientifica · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein-bound dinitrosyl iron complexes (DNICs) have been observed in prokaryotic and eukaryotic cells under nitric oxide (NO) stress. The identity of proteins that bind DNICs, however, still remains elusive. Here we demonstrate that iron-sulfur proteins are the major source of protein-bound DNICs formed in Escherichia coli cells under NO stress. Expression of recombinant iron-sulfur proteins, but not proteins without iron-sulfur clusters, almost doubles the amount of protein-bound DNICs formed in E. coli cells after NO exposure. Purification of recombinant proteins from the NO-exposed E. coli cells further confirms that iron-sulfur proteins, but not proteins without iron-sulfur clusters, are modified, forming protein-bound DNICs. Deletion of the iron-sulfur cluster assembly proteins IscA and SufA to block the [4Fe-4S] cluster biogenesis in E. coli cells largely eliminates the NO-mediated formation of protein-bound DNICs, suggesting that iron-sulfur clusters are mainly responsible for the NO-mediated formation of protein-bound DNICs in cells. Furthermore, depletion of the "chelatable iron pool" in wild-type E. coli cells effectively removes iron-sulfur clusters from proteins and concomitantly diminishes the NO-mediated formation of protein-bound DNICs, indicating that iron-sulfur clusters in proteins constitute at least part of the chelatable iron pool in cells.
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Registered trials
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