Evidence map›Paper›PMID 42626997›Full record

ArticleChembiochem : a European journal of chemical biology2026

ω-Hydroxyacid Dehydrogenases From Clostridium viride: Iron-Containing Biocatalysts With Biotechnological Potential.

Tarik Begic, Julia Hill, Jan L Stitzel, Lukas Knauer, Volker Schünemann, Markus Räschle, Berta M Martins, Antonio J Pierik

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Tarik BegicBiochemistry, Department of Chemistry, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0000-0001-9897-5700
Julia HillBiochemistry, Department of Chemistry, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0009-0003-9969-2958
Jan L StitzelBiochemistry, Department of Chemistry, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0009-0006-3324-1064
Lukas KnauerDepartment of Physics, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0009-0000-1839-0412
Volker SchünemannDepartment of Physics, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0000-0002-3162-1032
Markus RäschleDepartment of Molecular Genetics, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0000-0002-6737-7203
Berta M MartinsInstitut für Biologie, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID https://orcid.org/0000-0001-9250-000X
Antonio J PierikBiochemistry, Department of Chemistry, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID https://orcid.org/0000-0002-1509-6370

Funding

Deutsche Forschungsgemeinschaft 311771384Deutsche Forschungsgemeinschaft 397427223Deutsche Forschungsgemeinschaft 444947649
6 · The paper itself

Abstract

ω-Hydroxy and oxo acids are versatile platform chemicals, accessible via enzymes of the iron-containing alcohol dehydrogenase (FeADH) superfamily. Compared with well-characterized zinc-dependent ADHs, FeADHs producing such compounds remain poorly defined regarding assignment to genetic locus, biochemical and biophysical properties, and metal specificity. Here, we uncover two FeADHs from Clostridium viride: a highly selective 4-hydroxybutyrate dehydrogenase and a broad-spectrum 5-hydroxyvalerate dehydrogenase highly active on C5-C12 substrates, identified by purification from the native organism. Chemical synthesis of 5-oxovalerate enabled determination of kinetics for the physiological direction (V

Indexed as

BiotechnologyClostridiumIronBiocatalysisCrystallography, X-RayKineticsModels, MolecularNADSubstrate SpecificityIronNADalcohol dehydrogenasebiocatalysisbiochemistrychemistryClostridiumcrystal structureelectron paramagnetic resonance spectroscopyMössbauer spectroscopynonheme ironregioselectivity

Identifiers

PMID42626997
PMCPMC13495136

What OpenQuestion holds

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Registered trials

None linked

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.