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A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire
Open accessPreprint — published as 10.1126/sciadv.adg6689
Abstract
Aldehyde oxidoreductases (AOR) are tungsten enzymes catalysing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacterium Aromatoleum aromaticum (AOR Aa ) consists of three different subunits (AorABC) and utilizes NAD as electron acceptor. Here we reveal that the enzyme forms filaments of repeating AorAB protomers which are capped by a single NAD-binding AorC subunit, based on solving its structure via cryo-electron microscopy. The polyferredoxin-like subunit AorA oligomerizes to an electron-conducting nanowire that is decorated with enzymatically active and W-cofactor (W-co) containing AorB subunits. Our structure further reveals the binding mode of the native substrate benzoate in the AorB active site. This, together with QM:MM-based modelling for the coordination of the W-co, enables formulation of catalytic mechanism hypothesis that paves the way for further engineering of AOR for applications in synthetic biology and biotechnology.
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Metadata
- Authors
- Winiarska, A., Ramírez-Amador, F., Hege, D., Gemmecker, Y., Prinz, S., Hochberg, G., Heider, J., Szaleniec, M., & Schuller, J. M.
- Affiliations
- Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences (PL)
- Philipps University of Marburg (DE)
- Max Planck Institute of Biophysics (DE)
- Max Planck Institute for Terrestrial Microbiology (DE)
- Corresponding author
- Winiarska, Agnieszka
- Heider, Johann
- Szaleniec, Maciej
- Schuller, Jan Michael
- ORCID
- Venue
- Science Advances
- Publisher
- openRxiv
- Published
- 2023-01-23
- Volume
- 9
- Issue
- 22
- Pages
- eadg6689-eadg6689
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC10413684
- OpenAlex
- W4379184360
- Cited by
- 20
- References
- 1
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 6
- FWCI
- 1.47
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Science Advances (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CeON Repository (Centre for Evaluation in Education and Science) (submittedVersion, cc-by)
- Funders
- European Commission (00-00-I004/16, POWR .03.02.00-00-I004/16, 101075992, HORIZON2020, 00-I004/16, Project POWR.03.02.00-00-I004/16, POWR.03.02)
- Deutsche Forschungsgemeinschaft (SCHU 3364/1-1, He2190/15-1)
- Narodowym Centrum Nauki
- Infrastruktura PL-Grid
- Academic Computer Centre Cyfronet, AGH University of Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Keywords
- aldehyde oxidoreductase, tungsten enzymes, protein nanowires, electronic conduction, Aromatoleum aromaticum, enzyme oligomerization, cryo-EM structure, catalytic mechanism, denitrifying bacteria
- MeSH terms
- Aldehyde Dehydrogenase, Aldehyde Oxidoreductases, NAD, Tungsten, Cryoelectron Microscopy, Nanowires
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