ArticleScientific reports2024
Structure of recombinant formate dehydrogenase from Methylobacterium extorquens (MeFDH1).
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- An unexpected alternative viologen electron mediator site in tungsten-containing formate dehydrogenase.FEBS letters · 2026Article
- Heterologous production of tungsten-dependent formate dehydrogenase I from Methylorubrum extorquens in Escherichia coli reveals α-subunit maturation as the major bottleneck.Bioresources and bioprocessing · 2026Article
- Semiartificial COChemical reviews · 2026Review
- A tungsten-specific maturation pathway governs cofactor assembly of a COThe Journal of biological chemistry · 2026Article
- Techno-economic analysis of industrial-scale fermentation for formate dehydrogenase (FDH) production.Bioresources and bioprocessing · 2025Article
- Understanding Metal-Organic Framework Densification: Solvent Effects and the Growth of Colloidal Primary Nanoparticles in Monolithic ZIF-8.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Formate dehydrogenase (FDH) is critical for the conversion between formate and carbon dioxide. Despite its importance, the structural complexity of FDH and difficulties in the production of the enzyme have made elucidating its unique physicochemical properties challenging. Here, we purified recombinant Methylobacterium extorquens AM1 FDH (MeFDH1) and used cryo-electron microscopy to determine its structure. We resolved a heterodimeric MeFDH1 structure at a resolution of 2.8 Å, showing a noncanonical active site and a well-embedded Fe-S redox chain relay. In particular, the tungsten bis-molybdopterin guanine dinucleotide active site showed an open configuration with a flexible C-terminal cap domain, suggesting structural and dynamic heterogeneity in the enzyme.
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Registered trials
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