ArticleThe Journal of biological chemistry2009
An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalase-peroxidase (KatG).
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 99 citations in OpenAlex.
- Single-atom substitution redirects KatG reactivity from cofactor biogenesis to stereoselective sulfoxidation.Nature communications · 2026Article
- Heterologous expression of a heme-dependent catalase from Avicennia marina confers multi-stress tolerance in Escherichia coli for biotechnological applications.Scientific reports · 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
- Co-crystallization ofActa crystallographica. Section E, Crystallographic communications · 2023Article
- Isoniazid causes heart looping disorder in zebrafish embryos by the induction of oxidative stress.BMC pharmacology & toxicology · 2020Article
- Newly Developed Prodrugs and Prodrugs in Development; an Insight of the Recent Years.Molecules (Basel, Switzerland) · 2020Review
- Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.Biochemistry · 2018Article
- 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
- Ester-prodrugs of ethambutol control its antibacterial activity and provide rapid screening for mycobacterial hydrolase activity.Bioorganic & medicinal chemistry letters · 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
- Biological and quantitative-SAR evaluations, and docking studies of (E)-N -benzylidenebenzohydrazide analogues as potential antibacterial agents.EXCLI journal · 2016Article
- A High-Throughput Assay for Developing Inhibitors of PhoP, a Virulence Factor of Mycobacterium tuberculosis.Combinatorial chemistry & high throughput screening · 2016Article
- Predicting Ecological Roles in the Rhizosphere Using Metabolome and Transportome Modeling.PloS one · 2015Article
- Article
- Pulsed EPR distance measurements in soluble proteins by site-directed spin labeling (SDSL).Current protocols in protein science · 2013Article
- Isoniazid inhibits the heme-based reactivity of Mycobacterium tuberculosis truncated hemoglobin N.PloS one · 2013Article
- 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
- Chemotherapeutic interventions against tuberculosis.Pharmaceuticals (Basel, Switzerland) · 2012Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
A mechanism accounting for the robust catalase activity in catalase-peroxidases (KatG) presents a new challenge in heme protein enzymology. In Mycobacterium tuberculosis, KatG is the sole catalase and is also responsible for peroxidative activation of isoniazid, an anti-tuberculosis pro-drug. Here, optical stopped-flow spectrophotometry, rapid freeze-quench EPR spectroscopy both at the X-band and at the D-band, and mutagenesis are used to identify catalase reaction intermediates in M. tuberculosis KatG. In the presence of millimolar H2O2 at neutral pH, oxyferrous heme is formed within milliseconds from ferric (resting) KatG, whereas at pH 8.5, low spin ferric heme is formed. Using rapid freeze-quench EPR at X-band under both of these conditions, a narrow doublet radical signal with an 11 G principal hyperfine splitting was detected within the first milliseconds of turnover. The radical and the unique heme intermediates persist in wild-type KatG only during the time course of turnover of excess H2O2 (1000-fold or more). Mutation of Met255, Tyr229, or Trp107, which have covalently linked side chains in a unique distal side adduct (MYW) in wild-type KatG, abolishes this radical and the catalase activity. The D-band EPR spectrum of the radical exhibits a rhombic g tensor with dual gx values (2.00550 and 2.00606) and unique gy (2.00344) and gz values (2.00186) similar to but not typical of native tyrosyl radicals. Density functional theory calculations based on a model of an MYW adduct radical built from x-ray coordinates predict experimentally observed hyperfine interactions and a shift in g values away from the native tyrosyl radical. A catalytic role for an MYW adduct radical in the catalase mechanism of KatG is proposed.
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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.