ArticleRedox biology2018
Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.
Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 44 citations in OpenAlex.
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- Quercetin as a Dietary Supplementary Flavonoid Alleviates the Oxidative Stress Induced by Lead Toxicity in Male Wistar Rats.Nutrients · 2023Article
- Efflux-linked accelerated evolution of antibiotic resistance at a population edge.Molecular cell · 2022Article
- Characterization of the glutathione-dependent reduction of the peroxiredoxin 5 homolog PfAOP from Plasmodium falciparum.Protein science : a publication of the Protein Society · 2022Article
- The Yeast eIF2 Kinase Gcn2 Facilitates HApplied and environmental microbiology · 2021Article
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- Peroxiredoxins couple metabolism and cell division in an ultradian cycle.Nature chemical biology · 2021Article
- Article
- Fundc1-dependent mitophagy is obligatory to ischemic preconditioning-conferred renoprotection in ischemic AKI via suppression of Drp1-mediated mitochondrial fission.Redox biology · 2020Article
- Hyperoxidation of mitochondrial peroxiredoxin limits HThe EMBO journal · 2019Article
- Tanshinone IIA attenuates cardiac microvascular ischemia-reperfusion injury via regulating the SIRT1-PGC1α-mitochondrial apoptosis pathway.Cell stress & chaperones · 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 parameters between cytosolic 2-Cys peroxiredoxins, PRDX1 and PRDX2.Protein science : a publication of the Protein Society · 2019Article
- Identification of Antioxidant Proteins With Deep Learning From Sequence Information.Frontiers in pharmacology · 2018Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Redox-sensitive green fluorescent protein 2 (roGFP2) is a valuable tool for redox measurements in living cells. Here, we demonstrate that roGFP2 can also be used to gain mechanistic insights into redox catalysis in vivo. In vitro enzyme properties such as the rate-limiting reduction of wild type and mutant forms of the model peroxiredoxin PfAOP are shown to correlate with the ratiometrically measured degree of oxidation of corresponding roGFP2 fusion proteins. Furthermore, stopped-flow kinetic measurements of the oxidative half-reaction of PfAOP support the interpretation that changes in the roGFP2 signal can be used to map hyperoxidation-based inactivation of the attached peroxidase. Potential future applications of our system include the improvement of redox sensors, the estimation of absolute intracellular peroxide concentrations and the in vivo assessment of protein structure-function relationships that cannot easily be addressed with recombinant enzymes, for example, the effect of post-translational protein modifications on enzyme catalysis.
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