ArticleACS catalysis2019
Biocatalytic Carbon-Hydrogen and Carbon-Fluorine Bond Cleavage through Hydroxylation Promoted by a Histidyl-Ligated Heme Enzyme.
Article in ACS catalysis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Analysis and Risks of Emerging Contaminants and Microplastics in Natural and Treated Waters and Human Health: A Critical Review.Journal of xenobiotics · 2026Review
- A Dynamic Gate Enables Regioselective Hydroxylation of Free Arginine by a Non-Canonical Heme Enzyme.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Role of Propionate Side Chain in Heme-Containing Metalloenzymes.ACS organic & inorganic Au · 2025Review
- Substrate Analogs Implicate a Free Radical Pathway in Tyrosine Hydroxylase Catalysis.ACS catalysis · 2025Article
- Deciphering Tryptophan Oxygenation: Key Modulators of 2-Oxindole Formation in MarE.Angewandte Chemie (International ed. in English) · 2025Article
- Reasons why life on Earth rarely makes fluorine-containing compounds and their implications for the search for life beyond Earth.Scientific reports · 2024Article
- Combined spectroscopic and structural approaches to explore the mechanism of histidine-ligated heme-dependent aromatic oxygenases.Methods in enzymology · 2023Article
- A new regime of heme-dependent aromatic oxygenase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Molecular Rationale for Partitioning between C-H and C-F Bond Activation in Heme-Dependent Tyrosine Hydroxylase.Journal of the American Chemical Society · 2021Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- Carbon-fluorine bond cleavage mediated by metalloenzymes.Chemical Society reviews · 2020Review
- Crystal Structures of L-DOPA Dioxygenase fromBiochemistry · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
LmbB2 is a peroxygenase-like enzyme that hydroxylates L-tyrosine to L-3,4-dihydroxyphenylalanine (DOPA) in the presence of hydrogen peroxide. However, its heme cofactor is ligated by a proximal histidine, not cysteine. We show that LmbB2 can oxidize L-tyrosine analogs with ring-deactivated substituents such as 3-nitro-, fluoro-, chloro-, iodo-L-tyrosine. We also found that the 4-hydroxyl group of the substrate is essential for reacting with the heme-based oxidant and activating the aromatic C-H bond. The most interesting observation of this study was obtained with 3-fluoro-L-tyrosine as a substrate and mechanistic probe. The LmbB2-mediated catalytic reaction yielded two hydroxylated products with comparable populations,
Indexed as
Identifiers
What OpenQuestion holds
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.