ArticleJournal of the American Chemical Society2026
Active Site Structure and Mechanism of a Molybdenum Catechol Dehydroxylase.
Article in Journal of the American Chemical Society, 2026. 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
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Who cites it
1 citing paper in PubMed.
- Advances in the DMSO reductase family: From discovery to mechanism.Current opinion in chemical biology · 2026Review
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Authors and funding
8 authors.
Funding
Abstract
The dehydroxylation of catechols represents an important chemical transformation facilitated by gut bacteria in mammals. This reaction is catalyzed by pyranopterin molybdenum enzymes that belong to the DMSO reductase family. Despite their chemical and biological significance, the structure and mechanisms of catechol dehydroxylases remain uncharacterized. In this manuscript, we interrogated the active site structure of hydrocaffeic acid dehydroxylase from the gut bacterium
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Registered trials
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