ReviewBiotech (Basel (Switzerland))2026
Iron-Containing Alcohol Dehydrogenase from Hyperthermophiles.
Review in Biotech (Basel (Switzerland)), 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
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
1 citing paper in PubMed.
- ω-Hydroxyacid Dehydrogenases From Clostridium viride: Iron-Containing Biocatalysts With Biotechnological Potential.Chembiochem : a European journal of chemical biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Iron-containing alcohol dehydrogenases (Fe-ADHs) from hyperthermophiles represent a distinct class of oxidoreductases characterized by exceptional thermostability, catalytic versatility, and unique metal-dependent properties. Despite considerable sequence diversity, Fe-ADHs share conserved motifs and a two-domain architecture essential for iron coordination and NAD(P)H cofactor binding. Physiologically, these enzymes are predicted to function primarily in aldehyde detoxification and redox homeostasis, with some also participating in fermentative alcohol production. Their remarkable stability and catalytic efficiency highlight their potential as robust biocatalysts for high-temperature industrial bioprocesses. This review presents a comprehensive comparative analysis of the biophysical, biochemical, and kinetic properties of Fe-ADHs, focusing on their thermostability, metal ion specificity, and catalytic mechanisms, as well as highlighting their potential for industrial biocatalytic applications.
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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.