ArticleChemical science2016
Oxidation triggers extensive conjugation and unusual stabilization of two di-heme dication diradical intermediates: role of bridging group for electronic communication.
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed, 55 citations in OpenAlex.
- Electronic Coupling and Electrocatalysis in Redox Active Fused Iron Corroles.Inorganic chemistry · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MauG is a diheme enzyme that utilizes two covalently bound c-type hemes to catalyse the biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone. The two hemes are physically separated by 14.5 Å and a hole-hopping mechanism is proposed in which a tryptophan residue located between the hemes undergoes reversible oxidation and reduction to increase the effective electronic coupling element and enhance the rate of reversible electron transfer between the hemes in bis-Fe(iv) MauG. The present work describes the structure and spectroscopic investigation of 2e-oxidations of the synthetic diheme analogs in which two heme centers are covalently connected through a conjugated ethylene bridge that leads to the stabilization of two unusual
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Registered trials
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