ArticleBiochemistry2015
Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 69 citations in OpenAlex.
- Linoleic Hydroperoxides Are Potent Hyperoxidative Agents of Sensitive and Robust Typical 2-Cys Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2025Article
- Mitochondrial Peroxiredoxin 3 Is Rapidly Oxidized and Hyperoxidized by Fatty Acid Hydroperoxides.Antioxidants (Basel, Switzerland) · 2023Article
- Evidence that protein thiols are not primary targets of intracellular reactive oxygen species in growingFrontiers in microbiology · 2023Article
- Article
- The Catalase KatA Contributes to Microaerophilic HAntioxidants (Basel, Switzerland) · 2022Article
- Effects of Serine or Threonine in the Active Site of Typical 2-Cys Prx on Hyperoxidation Susceptibility and on Chaperone Activity.Antioxidants (Basel, Switzerland) · 2021Article
- Distinct HFrontiers in microbiology · 2021Article
- Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways inThe Journal of biological chemistry · 2020Article
- Thiol Peroxidases as Major Regulators of Intracellular Levels of Peroxynitrite in LiveAntioxidants (Basel, Switzerland) · 2020Article
- The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione.Antioxidants (Basel, Switzerland) · 2020Article
- Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.ACS catalysis · 2020Article
- Antioxidation and symbiotic nitrogen fixation function of prxA gene in Mesorhizobium huakuii.MicrobiologyOpen · 2019Article
- Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193.Free radical biology & medicine · 2019Article
- Triphenylphosphonium-Derived Protein Sulfenic Acid Trapping Agents: Synthesis, Reactivity, and Effect on Mitochondrial Function.Chemical research in toxicology · 2019Article
- Differential parameters between cytosolic 2-Cys peroxiredoxins, PRDX1 and PRDX2.Protein science : a publication of the Protein Society · 2019Article
- Tyrosine substitution of a conserved active-site histidine residue activates Plasmodium falciparum peroxiredoxin 6.Protein science : a publication of the Protein Society · 2019Article
- Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing.Biochemistry · 2018Article
- Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.Redox biology · 2018Article
- Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Antioxidants & redox signaling · 2018Article
- Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.Free radical biology & medicine · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Peroxiredoxins make up a ubiquitous family of cysteine-dependent peroxidases that reduce hydroperoxide or peroxynitrite substrates through formation of a cysteine sulfenic acid (R-SOH) at the active site. In the 2-Cys peroxiredoxins, a second (resolving) cysteine reacts with the sulfenic acid to form a disulfide bond. For all peroxiredoxins, structural rearrangements in the vicinity of the active site cysteine(s) are necessary to allow disulfide bond formation and subsequent reductive recycling. In this study, we evaluated the rate constants for individual steps in the catalytic cycle of Salmonella typhimurium AhpC. Conserved Trp residues situated close to both peroxidatic and resolving cysteines in AhpC give rise to large changes in fluorescence during the catalytic cycle. For recycling, AhpF very efficiently reduces the AhpC disulfide, with a single discernible step and a rate constant of 2.3 × 10(7) M(-1) s(-1). Peroxide reduction was more complex and could be modeled as three steps, beginning with a reversible binding of H2O2 to the enzyme (k1 = 1.36 × 10(8) M(-1) s(-1), and k-1 = 53 s(-1)), followed by rapid sulfenic acid generation (620 s(-1)) and then rate-limiting disulfide bond formation (75 s(-1)). Using bulkier hydroperoxide substrates with higher Km values, we found that different efficiencies (kcat/Km) for turnover of AhpC with these substrates are primarily caused by their slower rates of binding. Our findings indicate that this bacterial peroxiredoxin exhibits rates for both reducing and oxidizing parts of the catalytic cycle that are among the fastest observed so far for this diverse family of enzymes.
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