ArticleNature communications2020
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 85 citations in OpenAlex.
- Recent Progress in Understanding the Mechanism of Formate Dehydrogenases.Chembiochem : a European journal of chemical biology · 2026Review
- Room-temperature crystal structure of a metal-dependent W-formate dehydrogenase by serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- Understanding the Catalytic Determinant role of Diaphorase-Like Subunit in Formate Dehydrogenases via Redox Couples.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Semiartificial COChemical reviews · 2026Review
- Tracking the redox reaction of the iron enzyme ribonucleotide reductase using continuous SerialED and SFX.Structure (London, England : 1993) · 2026Article
- Structural Insights Into COAngewandte Chemie (International ed. in English) · 2026Article
- A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.Nature structural & molecular biology · 2025Article
- Article
- Stabilization of the catalytically active structure of a molybdenum-dependent formate dehydrogenase depends on a highly conserved lysine residue.The FEBS journal · 2025Article
- In vitro sulfuration of Rhodobacter capsulatus formate dehydrogenase.The Journal of biological chemistry · 2025Article
- Reversible enzyme-catalysed NADChemical science · 2025Article
- Cryo-EM reveals a composite flavobicluster electron bifurcation site in the Bfu family member NfnABC.Communications biology · 2025Article
- Structural determinants of oxygen resistance and ZnProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Functional expression of a Mo-dependent formate dehydrogenase in Escherichia coli under aerobic conditions.PloS one · 2025Article
- The energy metabolism ofApplied and environmental microbiology · 2024Article
- Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structure of recombinant formate dehydrogenase from Methylobacterium extorquens (MeFDH1).Scientific reports · 2024Article
- Exploiting the full potential of cryo-EM maps.BBA advances · 2024Article
- Structures and Electron Transport Paths in the Four Families of Flavin-Based Electron Bifurcation Enzymes.Sub-cellular biochemistry · 2024Review
- Selenium-More than Just a Fortuitous Sulfur Substitute in Redox Biology.Molecules (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enzymes is limited. Here we report the cryo-electron microscopic structures of the soluble Rhodobacter capsulatus FDH (RcFDH) as isolated and in the presence of reduced nicotinamide adenine dinucleotide (NADH). RcFDH assembles into a 360 kDa dimer of heterotetramers revealing a putative interconnection of electron pathway chains. In the presence of NADH, the RcFDH structure shows charging of cofactors, indicative of an increased electron load.
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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.