ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2011
The mechanism of formate oxidation by metal-dependent formate dehydrogenases.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 92 citations in OpenAlex.
- One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026Review
- Recent Progress in Understanding the Mechanism of Formate Dehydrogenases.Chembiochem : a European journal of chemical biology · 2026Review
- Semiartificial COChemical reviews · 2026Review
- A tungsten-specific maturation pathway governs cofactor assembly of a COThe Journal of biological chemistry · 2026Article
- Structural Insights Into COAngewandte Chemie (International ed. in English) · 2026Article
- Hinged Carboxylate in the Artificial Distal Pocket of an Iron Porphyrin Enhances COAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacement.Chemical science · 2024Article
- Structure of recombinant formate dehydrogenase from Methylobacterium extorquens (MeFDH1).Scientific reports · 2024Article
- Metal-Containing Formate Dehydrogenases, a Personal View.Molecules (Basel, Switzerland) · 2023Review
- Bioinspired Framework Catalysts: From Enzyme Immobilization to Biomimetic Catalysis.Chemical reviews · 2023Review
- Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal-Based Formate Dehydrogenase.Angewandte Chemie (International ed. in English) · 2023Article
- Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation.International journal of molecular sciences · 2022Article
- Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal-Dependent Formate Dehydrogenase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Spectroscopic and Structural Characterization of ReducedACS chemical biology · 2022Article
- Energetics for COThe journal of physical chemistry. B · 2022Article
- The good, the neutral, and the positive: buffer identity impacts CODalton transactions (Cambridge, England : 2003) · 2019Article
- Formation of Unstable and very Reactive Chemical Species Catalyzed by Metalloenzymes: A Mechanistic Overview.Molecules (Basel, Switzerland) · 2019Review
- Reaction mechanism of formate dehydrogenase studied by computational methods.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase.Journal of the American Chemical Society · 2017Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metal-dependent formate dehydrogenases (Fdh) from prokaryotic organisms are members of the dimethyl sulfoxide reductase family of mononuclear molybdenum-containing and tungsten-containing enzymes. Fdhs catalyze the oxidation of the formate anion to carbon dioxide in a redox reaction that involves the transfer of two electrons from the substrate to the active site. The active site in the oxidized state comprises a hexacoordinated molybdenum or tungsten ion in a distorted trigonal prismatic geometry. Using this structural model, we calculated the catalytic mechanism of Fdh through density functional theory tools. The simulated mechanism was correlated with the experimental kinetic properties of three different Fdhs isolated from three different Desulfovibrio species. Our studies indicate that the C-H bond break is an event involved in the rate-limiting step of the catalytic cycle. The role in catalysis of conserved amino acid residues involved in metal coordination and near the metal active site is discussed on the basis of experimental and theoretical results.
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