ArticleProceedings of the National Academy of Sciences of the United States of America2008
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
78 citing papers in PubMed, 160 citations in OpenAlex.
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- OxyR contributes to the oxidative stress capacity and virulence of hypervirulentFrontiers in cellular and infection microbiology · 2025Article
- Cold-adapted characteristics and gene knockout of alkyl hydroperoxide reductase subunit C in Antarctic Psychrobacter sp. ANT206.World journal of microbiology & biotechnology · 2024Article
- Comparative Genomic and Transcriptomic Analysis of Phenol Degradation and Tolerance inInternational journal of molecular sciences · 2023Article
- Harnessing redox proteomics to study metabolic regulation and stress response in lignin-fed Rhodococci.Biotechnology for biofuels and bioproducts · 2023Article
- Article
- Systematic monitoring of 2-Cys peroxiredoxin-derived redox signals unveiled its role in attenuating carbon assimilation rate.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021Article
- Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins.iScience · 2021Article
- Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation.Nature communications · 2021Article
- Distinct HFrontiers in microbiology · 2021Article
- Action of carvacrol in Salmonella Typhimurium biofilm: A proteomic study.Journal of applied biomedicine · 2020Article
- Ethanol in Combination with Oxidative Stress Significantly Impacts Mycobacterial Physiology.Journal of bacteriology · 2020Article
- Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways inThe Journal of biological chemistry · 2020Article
- Structure-function analyses of alkylhydroperoxidase D fromThe Journal of biological chemistry · 2020Article
- The Human PathogenFrontiers in cellular and infection microbiology · 2020Article
- The complete genome sequence of3 Biotech · 2019Article
- The interactome of 2-Cys peroxiredoxins in Plasmodium falciparum.Scientific reports · 2019Article
18 more citing papers are in PubMed but not listed here.
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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that are involved in peroxide scavenging and/or the regulation of peroxide signaling in eukaryotes. Despite their prevalence, very few Prxs have been reliably characterized in terms of their substrate specificity profile and redox potential even though these values are important for gaining insight into physiological function. Here, we present such studies focusing on Salmonella typhimurium alkyl hydroperoxide reductase C component (StAhpC), an enzyme that has proven to be an excellent prototype of this largest and most widespread class of Prxs that includes mammalian Prx I-Prx IV. The catalytic efficiencies of StAhpC (k(cat)/K(m)) are >10(7) M(-1).s(-1) for inorganic and primary hydroperoxide substrates and approximately 100-fold less for tertiary hydroperoxides, with the difference being exclusively caused by changes in K(m). The oxidative inactivation of AhpC through reaction with a second molecule of peroxide shows parallel substrate specificity. The midpoint reduction potential of StAhpC is determined to be -178 +/- 0.4 mV, a value much higher than most other thiol-based redox proteins. The relevance of these results for our understanding of Prx and the physiological role of StAhpC is discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.