ArticleNature structural & molecular biology2009
Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 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
33 citing papers in PubMed, 83 citations in OpenAlex.
- Thr-to-Ala Mutation Leads to a Larger Aromatic Pair and Reduced Packing Density in α1,α3-Helices during Thioredoxin Cold Adaptation.ACS omega · 2024Article
- Distinct or Overlapping Areas of Mitochondrial Thioredoxin 2 May Be Used for Its Covalent and Strong Non-Covalent Interactions with Protein Ligands.Antioxidants (Basel, Switzerland) · 2023Article
- Antioxidant Therapy in Cancer: Rationale and Progress.Antioxidants (Basel, Switzerland) · 2022Review
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Methods to identify the substrates of thiol-disulfide oxidoreductases.Protein science : a publication of the Protein Society · 2019Review
- Compound kushen injection suppresses human acute myeloid leukaemia by regulating the Prdxs/ROS/Trx1 signalling pathway.Journal of experimental & clinical cancer research : CR · 2018Article
- Mechanical architecture and folding of E. coli type 1 pilus domains.Nature communications · 2018Article
- Conformational dynamics and enzyme evolution.Journal of the Royal Society, Interface · 2018Review
- Ancient thioredoxins evolved to modern-day stability-function requirement by altering native state ensemble.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins.Nature structural & molecular biology · 2017Article
- Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants.Scientific reports · 2017Article
- Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA.The Journal of biological chemistry · 2015Article
- Probing the effect of force on HIV-1 receptor CD4.ACS nano · 2014Article
- Probing protein multidimensional conformational fluctuations by single-molecule multiparameter photon stamping spectroscopy.The journal of physical chemistry. B · 2014Article
- Disulfide bond formation in prokaryotes: history, diversity and design.Biochimica et biophysica acta · 2014Review
- Role of substrate unbinding in Michaelis-Menten enzymatic reactions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Elasticity, structure, and relaxation of extended proteins under force.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Nature protocols · 2013Article
Corrections and comments
- Erratum issuedGaucher, Eric [corrected to Gaucher, Eric A]
Authors and funding
19 authors at 7 institutions in 5 countries.
Funding
Abstract
Thioredoxins (Trxs) are oxidoreductase enzymes, present in all organisms, that catalyze the reduction of disulfide bonds in proteins. By applying a calibrated force to a substrate disulfide, the chemical mechanisms of Trx catalysis can be examined in detail at the single-molecule level. Here we use single-molecule force-clamp spectroscopy to explore the chemical evolution of Trx catalysis by probing the chemistry of eight different Trx enzymes. All Trxs show a characteristic Michaelis-Menten mechanism that is detected when the disulfide bond is stretched at low forces, but at high forces, two different chemical behaviors distinguish bacterial-origin from eukaryotic-origin Trxs. Eukaryotic-origin Trxs reduce disulfide bonds through a single-electron transfer reaction (SET), whereas bacterial-origin Trxs show both nucleophilic substitution (S(N)2) and SET reactions. A computational analysis of Trx structures identifies the evolution of the binding groove as an important factor controlling the chemistry of Trx catalysis.
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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.