ArticleChemistry (Weinheim an der Bergstrasse, Germany)2014
Experimental and computational evidence for the mechanism of intradiol catechol dioxygenation by non-heme iron(III) complexes.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 22 citations in OpenAlex.
- Charge Maintenance during Catalysis in Nonheme Iron Oxygenases.ACS catalysis · 2022Article
- Biological Inspirations: Iron Complexes Mimicking the Catechol Dioxygenases.Materials (Basel, Switzerland) · 2021Review
- Advances in Sustainable Catalysis: A Computational Perspective.Frontiers in chemistry · 2019Review
- Does Substrate Positioning Affect the Selectivity and Reactivity in the Hectochlorin Biosynthesis Halogenase?Frontiers in chemistry · 2018Article
- Electronic, Magnetic, and Redox Properties and OInorganic chemistry · 2017Article
- Mono- and binuclear non-heme iron chemistry from a theoretical perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Alkyl Chain Growth on a Transition Metal Center: How Does Iron Compare to Ruthenium and Osmium?International journal of molecular sciences · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Catechol intradiol dioxygenation is a unique reaction catalyzed by iron-dependent enzymes and non-heme iron(III) complexes. The mechanism by which these systems activate dioxygen in this important metabolic process remains controversial. Using a combination of kinetic measurements and computational modelling of multiple iron(III) catecholato complexes, we have elucidated the catechol cleavage mechanism and show that oxygen binds the iron center by partial dissociation of the substrate from the iron complex. The iron(III) superoxide complex that is formed subsequently attacks the carbon atom of the substrate by a rate-determining C-O bond formation step.
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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.