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Volume 6
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10.3390/reactions6030046
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This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Article

An Iron-Dependent Alcohol Dehydrogenase Is Involved in Ethanol Metabolism of Aromatoleum aromaticum

by
Yvonne Gemmecker
1,
Iris Schall
1,
Andreas Seubert
2,
Nicole Paczia
3 and
Johann Heider
1,4,*
1
Laboratory for Microbial Biochemistry, Philipps University of Marburg, 35043 Marburg, Germany
2
Department of Chemistry, Philipps University Marburg, 35043 Marburg, Germany
3
Core Facility for Metabolomics and Small Molecule Mass Spectrometry, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany
4
LOEWE-Center for Synthetic Microbiology, 35043 Marburg, Germany
*
Author to whom correspondence should be addressed.
Reactions 2025, 6(3), 46; https://doi.org/10.3390/reactions6030046 (registering DOI)
Submission received: 2 July 2025 / Revised: 29 August 2025 / Accepted: 30 August 2025 / Published: 1 September 2025
(This article belongs to the Special Issue Feature Papers in Reactions in 2025)
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Abstract

The NAD+-dependent alcohol dehydrogenase AdhB from Aromatoleum aromaticum EbN1 belongs to family III of Fe-dependent alcohol dehydrogenases. It was recombinantly produced in Escherichia coli and biochemically characterized, showing activity only with ethanol or n-propanol. The enzyme contained substoichiometric amounts of Fe, Zn, and Ni and a yet unidentified nucleotide-like cofactor, as indicated by mass spectrometric data. As suggested by its narrow substrate spectrum and complementation of a related species to growth on ethanol, the most probable physiological function of AdhB is the oxidation of short aliphatic alcohols such as ethanol or n-propanol. The enzyme also exhibits a very high tolerance to ethanol and n-propanol, showing moderately substrate-inhibited Michaelis–Menten kinetics up to concentrations of 20% (v/v). AdhB can also be applied biotechnologically to convert acetate to ethanol in coupled enzyme assays with the tungsten enzyme aldehyde oxidoreductase, showing activity with either another aldehyde or pre-reduced benzyl viologen as electron donors.
Keywords: alcohol dehydrogenase; enzyme kinetics; alcohol tolerance; aliphatic alcohols; growth experiments; coupled enzyme assay alcohol dehydrogenase; enzyme kinetics; alcohol tolerance; aliphatic alcohols; growth experiments; coupled enzyme assay
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MDPI and ACS Style

Gemmecker, Y.; Schall, I.; Seubert, A.; Paczia, N.; Heider, J. An Iron-Dependent Alcohol Dehydrogenase Is Involved in Ethanol Metabolism of Aromatoleum aromaticum. Reactions 2025, 6, 46. https://doi.org/10.3390/reactions6030046

AMA Style

Gemmecker Y, Schall I, Seubert A, Paczia N, Heider J. An Iron-Dependent Alcohol Dehydrogenase Is Involved in Ethanol Metabolism of Aromatoleum aromaticum. Reactions. 2025; 6(3):46. https://doi.org/10.3390/reactions6030046

Chicago/Turabian Style

Gemmecker, Yvonne, Iris Schall, Andreas Seubert, Nicole Paczia, and Johann Heider. 2025. "An Iron-Dependent Alcohol Dehydrogenase Is Involved in Ethanol Metabolism of Aromatoleum aromaticum" Reactions 6, no. 3: 46. https://doi.org/10.3390/reactions6030046

APA Style

Gemmecker, Y., Schall, I., Seubert, A., Paczia, N., & Heider, J. (2025). An Iron-Dependent Alcohol Dehydrogenase Is Involved in Ethanol Metabolism of Aromatoleum aromaticum. Reactions, 6(3), 46. https://doi.org/10.3390/reactions6030046

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