ArticleBiochemistry2011
Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 51 citations in OpenAlex.
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- Mechanism-based peroxiredoxin 3 inhibitors exploit a covalent warhead for cancer therapy.Science advances · 2025Article
- High-quality genome of a novel Thermosynechococcaceae species from Namibia and characterization of its protein expression patterns at elevated temperatures.MicrobiologyOpen · 2024Article
- The multiplicity of thioredoxin systems meets the specific lifestyles of Clostridia.PLoS pathogens · 2024Article
- Modelling the Decamerisation Cycle of PRDX1 and the Inhibition-like Effect on Its Peroxidase Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Anaerobic RSH-dependent tellurite reduction contributes to Escherichia coli tolerance against tellurite.Biological research · 2022Article
- Unique Cellular and Biochemical Features of Human Mitochondrial Peroxiredoxin 3 Establish the Molecular Basis for Its Specific Reaction with Thiostrepton.Antioxidants (Basel, Switzerland) · 2021Article
- Engineering regulatory networks for complex phenotypes in E. coli.Nature communications · 2020Article
- Using Bacterial Transcriptomics to Investigate Targets of Host-Bacterial Interactions in Caenorhabditis elegans.Scientific reports · 2019Article
- Aromatic Residues at the Dimer-Dimer Interface in the Peroxiredoxin Tsa1 Facilitate Decamer Formation and Biological Function.Chemical research in toxicology · 2019Article
- Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing.Biochemistry · 2018Article
- Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Antioxidants & redox signaling · 2018Article
- The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?Antioxidants & redox signaling · 2017Review
- Peroxiredoxin Catalysis at Atomic Resolution.Structure (London, England : 1993) · 2016Article
- Comprehensively Characterizing the Thioredoxin Interactome In Vivo Highlights the Central Role Played by This Ubiquitous Oxidoreductase in Redox Control.Molecular & cellular proteomics : MCP · 2016Article
- X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action.Journal of structural biology · 2016Article
- A Kinetic Platform to Determine the Fate of Hydrogen Peroxide in Escherichia coli.PLoS computational biology · 2015Article
- Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.Trends in biochemical sciences · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In Escherichia coli, bacterioferritin comigratory protein (BCP) is a peroxiredoxin (Prx) that catalyzes the reduction of H(2)O(2) and organic hydroperoxides. This protein, along with plant PrxQ, is a founding member of one of the least studied subfamilies of Prxs. Recent structural data have suggested that proteins in the BCP/PrxQ group can exist as monomers or dimers; we report here that, by analytical ultracentrifugation, both oxidized and reduced E. coli BCP behave as monomers in solution at concentrations as high as 200 μM. Unexpectedly, thioredoxin (Trx1)-dependent peroxidase assays conducted by stopped-flow spectroscopy demonstrated that V(max,app) increases with increasing Trx1 concentrations, indicating a nonsaturable interaction (K(m) > 100 μM). At a physiologically reasonable Trx1 concentration of 10 μM, the apparent K(m) value for H(2)O(2) is ~80 μM, and overall, the V(max)/K(m) for H(2)O(2), which remains constant at the various Trx1 concentrations (consistent with a ping-pong mechanism), is ~1.3 × 10(4) M(-1) s(-1). Our kinetic analyses demonstrated that BCP can utilize a variety of reducing substrates, including Trx1, Trx2, Grx1, and Grx3. BCP exhibited a high redox potential of -145.9 ± 3.2 mV, the highest to date observed for a Prx. Moreover, BCP exhibited a broad peroxide specificity, with comparable rates for H(2)O(2) and cumene hydroperoxide. We determined a pK(a) of ~5.8 for the peroxidatic cysteine (Cys45) using both spectroscopic and activity titration data. These findings support an important role for BCP in interacting with multiple substrates and remaining active under highly oxidizing cellular conditions, potentially serving as a defense enzyme of last resort.
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