ReviewMolecules (Basel, Switzerland)2023
Metal-Containing Formate Dehydrogenases, a Personal View.
Review in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026Review
- Cu and SnOChemSusChem · 2026Article
- Synthesis and Characterization of Rubisco-Magnesium Complexes for Potential Gas Adsorption Applications.ACS omega · 2026Article
- In vitro sulfuration of Rhodobacter capsulatus formate dehydrogenase.The Journal of biological chemistry · 2025Article
- Obligately Tungsten-Dependent Enzymes─Catalytic Mechanisms, Models and Applications.Biochemistry · 2025Review
- Synthetic Challenges toward Modeling Formate Dehydrogenases Using [WInorganic chemistry · 2024Article
- Active Site Characterization of aInorganic chemistry · 2024Article
- Selenium-More than Just a Fortuitous Sulfur Substitute in Redox Biology.Molecules (Basel, Switzerland) · 2023Review
- The History of Animal and Plant Sulfite Oxidase-A Personal View.Molecules (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Mo/W-containing formate dehydrogenases (FDH) catalyzes the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active sites. The metal-containing FDHs are members of the dimethylsulfoxide reductase family of mononuclear molybdenum cofactor (Moco)- or tungsten cofactor (Wco)-containing enzymes. In these enzymes, the active site in the oxidized state comprises a Mo or W atom present in the bis-Moco, which is coordinated by the two dithiolene groups from the two MGD moieties, a protein-derived SeCys or Cys, and a sixth ligand that is now accepted as being a sulfido group. SeCys-containing enzymes have a generally higher turnover number than Cys-containing enzymes. The analogous chemical properties of W and Mo, the similar active sites of W- and Mo-containing enzymes, and the fact that W can replace Mo in some enzymes have led to the conclusion that Mo- and W-containing FDHs have the same reaction mechanism. Details of the catalytic mechanism of metal-containing formate dehydrogenases are still not completely understood and have been discussed here.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.