ArticleJournal of the American Chemical Society2017
Probing Ligand Exchange in the P450 Enzyme CYP121 from Mycobacterium tuberculosis: Dynamic Equilibrium of the Distal Heme Ligand as a Function of pH and Temperature.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Single-atom substitution redirects KatG reactivity from cofactor biogenesis to stereoselective sulfoxidation.Nature communications · 2026Article
- Molecular Basis for Peptide Nitration by a Novel Cytochrome P450 Enzyme in RiPP Biosynthesis.ACS catalysis · 2025Article
- Mechanistic Perspective on C-N and C-S Bond Construction Catalyzed by Cytochrome P450 Enzymes.ACS bio & med chem Au · 2025Review
- Proton-Induced Switching of Paramagnetism: Reversible Conversion between a Low and High Spin CoJournal of the American Chemical Society · 2025Article
- Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.Angewandte Chemie (International ed. in English) · 2024Article
- Cobalt(II)-Substituted Cysteamine Dioxygenase Oxygenation Proceeds through a Cobalt(III)-Superoxo Complex.Journal of the American Chemical Society · 2024Article
- Article
- Deep residual networks for crystallography trained on synthetic data.Acta crystallographica. Section D, Structural biology · 2024Article
- In Situ Structural Observation of a Substrate- and Peroxide-Bound High-Spin Ferric-Hydroperoxo Intermediate in the P450 Enzyme CYP121.Journal of the American Chemical Society · 2023Article
- Low molecular weight ligands bind to CYP3A4 via a branched induced fit mechanism: Implications for OArchives of biochemistry and biophysics · 2023Article
- Charge Maintenance during Catalysis in Nonheme Iron Oxygenases.ACS catalysis · 2022Article
- Light-Activated Electron Transfer and Catalytic Mechanism of Carnitine Oxidation by Rieske-Type Oxygenase from Human Microbiota.Angewandte Chemie (International ed. in English) · 2021Article
- Heme Binding to HupZ with a C-Terminal Tag from Group A Streptococcus.Molecules (Basel, Switzerland) · 2021Article
- Surface hydrophobics mediate functional dimerization of CYP121A1 of Mycobacterium tuberculosis.Scientific reports · 2021Article
- Anti-Tubercular Properties of 4-Amino-5-(4-Fluoro-3- Phenoxyphenyl)-4Antibiotics (Basel, Switzerland) · 2020Article
- Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates.The Journal of biological chemistry · 2020Article
- Multiple drug binding modes in Mycobacterium tuberculosis CYP51B1.Journal of inorganic biochemistry · 2020Article
- Substrate-Assisted Hydroxylation andACS catalysis · 2020Article
- Biocatalytic Carbon-Hydrogen and Carbon-Fluorine Bond Cleavage through Hydroxylation Promoted by a Histidyl-Ligated Heme Enzyme.ACS catalysis · 2019Article
- Formation and Cleavage of C-C Bonds by Enzymatic Oxidation-Reduction Reactions.Chemical reviews · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
CYP121 is a cytochrome P450 enzyme from Mycobacterium tuberculosis that catalyzes the formation of a C-C bond between the aromatic groups of its cyclodityrosine substrate (cYY). The crystal structure of CYP121 in complex with cYY reveals that the solvent-derived ligand remains bound to the ferric ion in the enzyme-substrate complex. Whereas in the generally accepted P450 mechanism, binding of the primary substrate in the active-site triggers the release of the solvent-derived ligand, priming the metal center for reduction and subsequent O
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