ArticleFrontiers in chemistry2018
Mn-Mimochrome VI
Article in Frontiers in chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- Biohybrid materials comprising an artificial peroxidase and differently shaped gold nanoparticles.Nanoscale advances · 2024Article
- Dye Decolorization by a Miniaturized Peroxidase Fe-MimochromeVI*a.International journal of molecular sciences · 2023Article
- Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase.International journal of molecular sciences · 2023Article
- Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme.RSC advances · 2022Article
- Rigidifying aACS catalysis · 2021Article
- Unravelling the Structure of the Tetrahedral Metal-Binding Site in METP3 through an Experimental and Computational Approach.Molecules (Basel, Switzerland) · 2021Article
- Use of an Artificial Miniaturized Enzyme in Hydrogen Peroxide Detection by Chemiluminescence.Sensors (Basel, Switzerland) · 2020Article
- Unlocking the therapeutic potential of artificial metalloenzymes.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Manganese-porphyrins are important tools in catalysis, due to their capability to promote a wide variety of synthetically valuable transformations. Despite their great reactivity, the difficulties to control the reaction selectivity and to protect the catalyst from self-degradation hamper their practical application. Compared to small-molecule porphyrin complexes, metalloenzymes display remarkable features, because the reactivity of the metal center is finely modulated by a complex interplay of interactions within the protein matrix. In the effort to combine the catalytic potential of manganese porphyrins with the unique properties of biological catalysts, artificial metalloenzymes have been reported, mainly by incorporation of manganese-porphyrins into native protein scaffolds. Here we describe the spectroscopic and catalytic properties of Mn-Mimochrome VI
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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.