ArticleThe Journal of biological chemistry2013
Mechanism of [4Fe-4S](Cys)4 cluster nitrosylation is conserved among NO-responsive regulators.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 70 citations in OpenAlex.
- Harnessing gasotransmitters for orthopaedic infection therapy: Mechanisms and advanced delivery platforms.Bioactive materials · 2027Review
- ArnR binds a [4Fe-4S] cluster and indirectly senses anaerobicity in Corynebacteria.Metallomics : integrated biometal science · 2025Article
- Nitrite Causes Nitrosative Stress to Iron Sulfur Clusters.Journal of the American Chemical Society · 2025Article
- Article
- WhiB-like proteins: Diversity of structure, function and mechanism.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Val43 residue of NsrR is crucial for the nitric oxide response ofMicrobiology spectrum · 2024Article
- Nitric oxide is a host cue for Salmonella Typhimurium systemic infection in mice.Communications biology · 2023Article
- The Elusive Mononitrosylated [FeAngewandte Chemie (International ed. in English) · 2022Article
- Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021Review
- Transcriptional and Post-transcriptional Control of the Nitrate Respiration in Bacteria.Frontiers in molecular biosciences · 2021Review
- The Central Role of Redox-Regulated Switch Proteins in Bacteria.Frontiers in molecular biosciences · 2021Review
- Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.Nucleic acids research · 2020Article
- Structural and functional insight into the Mycobacterium tuberculosis protein PrpR reveals a novel type of transcription factor.Nucleic acids research · 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
- Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe-4S] NsrR.Chemical communications (Cambridge, England) · 2018Article
- Biochemical characterization and essentiality ofThe Journal of biological chemistry · 2018Article
- Article
- Structure of a Wbl protein and implications for NO sensing by M. tuberculosis.Nature communications · 2017Article
- Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.Angewandte Chemie (International ed. in English) · 2016Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
The Fumarate nitrate reduction (FNR) regulator from Escherichia coli controls expression of >300 genes in response to O2 through reaction with its [4Fe-4S] cluster cofactor. FNR is the master switch for the transition between anaerobic and aerobic respiration. In response to physiological concentrations of nitric oxide (NO), FNR also regulates genes, including the nitrate reductase (nar) operon, a major source of endogenous cellular NO, and hmp, which encodes an NO-detoxifying enzyme. Here we show that the [4Fe-4S] cluster of FNR reacts rapidly in a multiphasic reaction with eight NO molecules. Oxidation of cluster sulfide ions (S(2-)) to sulfane (S(0)) occurs, some of which remains associated with the protein as Cys persulfide. The nitrosylation products are similar to a pair of dinuclear dinitrosyl iron complexes, [Fe(I)2(NO)4(Cys)2](0), known as Roussin's red ester. A similar reactivity with NO was reported for the Wbl family of [4Fe-4S]-containing proteins found only in actinomycetes, such as Streptomyces and Mycobacteria. These results show that NO reacts via a common mechanism with [4Fe-4S] clusters in phylogenetically unrelated regulatory proteins that, although coordinated by four Cys residues, have different cluster environments. The reactivity of E. coli FNR toward NO, in addition to its sensitivity toward O2, is part of a hierarchal network that monitors, and responds to, NO, both endogenously generated and exogenously derived.
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