ArticleThe Journal of biological chemistry2012
Direct oxidation of the [2Fe-2S] cluster in SoxR protein by superoxide: distinct differential sensitivity to superoxide-mediated signal transduction.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Deciphering the genetic background of an industrial 2-ketogluconic acid-producing strain Pseudomonas plecoglossicida JUIM01 using whole-genome sequencing.Biotechnology for biofuels and bioproducts · 2026Article
- Electrochemistry as a Tool for Redox-Based Bio-Information Processing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The Mar, Sox, and Rob Systems.EcoSal Plus · 2023Review
- Synthetic biology and bioelectrochemical tools for electrogenetic system engineering.Science advances · 2022Article
- Interaction of Periplasmic Fab Production and Intracellular Redox Balance inACS synthetic biology · 2022Article
- Bacterial MerR family transcription regulators: activationby distortion.Acta biochimica et biophysica Sinica · 2022Review
- Exposure to stressors and antimicrobials induces cell-autonomous ultrastructural heterogeneity of an intracellular bacterial pathogen.Frontiers in cellular and infection microbiology · 2022Article
- Role of phenazine-enzyme physiology for current generation in a bioelectrochemical system.Microbial biotechnology · 2021Article
- MarA, RamA, and SoxS as Mediators of the Stress Response: Survival at a Cost.Frontiers in microbiology · 2020Article
- Gene networks that compensate for crosstalk with crosstalk.Nature communications · 2019Article
- Redox Is a Global Biodevice Information Processing Modality.Proceedings of the IEEE. Institute of Electrical and Electronics Engineers · 2019Article
- Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily.Scientific reports · 2016Article
- DNA Charge Transport: from Chemical Principles to the Cell.Cell chemical biology · 2016Review
- Structural, Functional, and Immunogenic Insights on Cu,Zn Superoxide Dismutase Pathogenic Virulence Factors from Neisseria meningitidis and Brucella abortus.Journal of bacteriology · 2015Article
- Transcription Factors That Defend Bacteria Against Reactive Oxygen Species.Annual review of microbiology · 2015Review
- An overview of mechanisms of redox signaling.Journal of molecular and cellular cardiology · 2014Review
- F-box and leucine-rich repeat protein 5 (FBXL5): sensing intracellular iron and oxygen.Journal of inorganic biochemistry · 2014Review
- Comparative study of SoxR activation by redox-active compounds.Molecular microbiology · 2013Article
- Antimicrobial strategies centered around reactive oxygen species--bactericidal antibiotics, photodynamic therapy, and beyond.FEMS microbiology reviews · 2013Review
- The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium.Nature reviews. Microbiology · 2013Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The [2Fe-2S] transcription factor SoxR is activated by reversible one-electron oxidation of its [2Fe-2S] cluster, leading to enhanced production of various antioxidant proteins through induction of the soxRS regulon in Escherichia coli. Recently, there has been considerable debate about whether superoxide (O(2)(•)) activates SoxR directly. To elucidate the underlying activation mechanism, we investigated SoxR interaction with O(2)(•) using pulse radiolysis. Radiolytically generated hydrated electrons reduced the oxidized form of the [2Fe-2S] cluster of SoxR within 2 μs. A subsequent increase in absorption in the visible region corresponding to reoxidation of the [2Fe-2S] cluster was observed on a time scale of milliseconds. Addition of human copper/zinc superoxide dismutase inhibited this delayed oxidation in a concentration-dependent fashion (I(50) = 1.0 μm), indicating that O(2)(•) oxidized the reduced form of SoxR directly. The second-order rate constant of this process was estimated to be 5 × 10(8) m(-1) s(-1). A similar result was observed after pulse radiolysis of Pseudomonas aeruginosa SoxR. However, superoxide dismutase inhibited the oxidation of reduced SoxR much more effectively in P. aeruginosa, even at a lower concentration (I(50) = 80 nm), indicating that the soxRS response is much more sensitive to O(2)(•) in E. coli than in P. aeruginosa. These results suggest that SoxR proteins play a distinct regulatory role in the activation of O(2)(•).
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