ArticleJournal of the American Chemical Society2010
A radical on the Met-Tyr-Trp modification required for catalase activity in catalase-peroxidase is established by isotopic labeling and site-directed mutagenesis.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 41 citations in OpenAlex.
- Single-atom substitution redirects KatG reactivity from cofactor biogenesis to stereoselective sulfoxidation.Nature communications · 2026Article
- Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.Angewandte Chemie (International ed. in English) · 2024Article
- Catalase-peroxidase (KatG): a potential frontier in tuberculosis drug development.Critical reviews in biochemistry and molecular biology · 2024Review
- Highly Sensitive Labeling, Clickable Functionalization, and Glycoengineering of the MUC1 Neighboring System.JACS Au · 2024Article
- A new regime of heme-dependent aromatic oxygenase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.The Journal of biological chemistry · 2017Article
- Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.Journal of the American Chemical Society · 2016Article
- Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.Biochemistry · 2016Article
- Reverse Electron Transfer Completes the Catalytic Cycle in a 2,3,5-Trifluorotyrosine-Substituted Ribonucleotide Reductase.Journal of the American Chemical Society · 2015Article
- The 2.2 Å resolution structure of the catalase-peroxidase KatG from Synechococcus elongatus PCC7942.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Specific function of the Met-Tyr-Trp adduct radical and residues Arg-418 and Asp-137 in the atypical catalase reaction of catalase-peroxidase KatG.The Journal of biological chemistry · 2012Article
- High conformational stability of secreted eukaryotic catalase-peroxidases: answers from first crystal structure and unfolding studies.The Journal of biological chemistry · 2012Article
- Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.Journal of the American Chemical Society · 2011Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A transient tyrosyl-like radical with a narrow doublet X-band EPR signal is present during catalase turnover by Mycobacterium tuberculosis catalase-peroxidase (KatG). Labeling of KatG with beta-methylene-deuterated tyrosine causes a collapse of the doublet to a singlet, while for 3,5-ring-deuterated tyrosine-labeled enzyme, no changes occur in the EPR signal. Except for the replacement Tyr229Phe, all other single-tyrosine mutants of KatG exhibit the same narrow doublet EPR signal and catalase activity similar to that of the wild-type enzyme. These findings confirm that this catalytically competent radical is associated with Tyr229, whose 3' and 5' protons are replaced as a result of cross-links with neighboring Met255 and Trp107 side chains in the post-translationally modified enzyme containing a distal-side Met255-Tyr229-Trp107 adduct.
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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.