Functional expression of a Mo-dependent formate dehydrogenase in Escherichia coli under aerobic conditions
A member of the oxygen-tolerant subclass of complex FDH showed stable formate oxidation activity when expressed in the heterologous host E. coli, a model organism of biotechnology. The integration of the operon in the chromosome offers the possibility of structure/function studies and activity enhancements through in vivo mutagenesis, which can also be applied to CO2 reduction in appropriate selection hosts.
Authors
- David Roche (ORCID: https://orcid.org/0000-0003-2366-0311)
- Mélodie Cadillon
- Ivan Dubois
- Volker Döring (ORCID: https://orcid.org/0000-0002-9453-6572)
- Valérie Delmas
- Madeleine Bouzon (ORCID: https://orcid.org/0000-0002-9581-6584)
- Marion Schulz
- Emilie Pateau
- Anne Berger
Institutions
- Centre National de la Recherche Scientifique (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Université Paris-Saclay (FR)
- Genoscope (FR)
- CEA Paris-Saclay (FR)
Publication Details
- Journal
- PLoS ONE
- Published
- 2025-10-29
- DOI
- https://doi.org/10.1371/journal.pone.0334613
- Citations
- 1
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.36