ArticleProceedings of the National Academy of Sciences of the United States of America2015
Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 49 citations in OpenAlex.
- Semiartificial COChemical reviews · 2026Review
- Emerging roles of pterins as signaling molecules in bacteria.Biochemical Society transactions · 2026Review
- Studies of the membrane-bound flavocytochrome MsrQ flavin mononucleotide (FMN)-binding site reveal an unexpected ubiquinone cofactor.The FEBS journal · 2025Article
- Molybdenum Cofactor Model Reveals Remarkable Redox Activity at Both Molybdenum and the Pyranopterin Dithiolene Ligand.Journal of the American Chemical Society · 2025Article
- Parameterization and quantification of two key operando physio-chemical descriptors for water-assisted electro-catalytic organic oxidation.Nature communications · 2024Article
- Practical Guide to Large Amplitude Fourier-Transformed Alternating Current Voltammetry-What, How, and Why.ACS measurement science au · 2024Article
- Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis.Molecules (Basel, Switzerland) · 2023Review
- Enzymatic and Microbial Electrochemistry: Approaches and Methods.ACS measurement science au · 2022Review
- Protonation and Non-Innocent Ligand Behavior in Pyranopterin Dithiolene Molybdenum Complexes.Inorganic chemistry · 2022Article
- Polyoxometalate Nanoparticles as a Potential Glioblastoma Therapeutic via Lipid-Mediated Cell Death.International journal of molecular sciences · 2022Article
- Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.Metal ions in life sciences · 2020Article
- Deconvolution of reduction potentials of formate dehydrogenase from Cupriavidus necator.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Modeling Pyran Formation in the Molybdenum Cofactor: Protonation of Quinoxalyl-Dithiolene Promoting Pyran Cyclization.Inorganic chemistry · 2019Article
- Implications of Pyran Cyclization and Pterin Conformation on Oxidized Forms of the Molybdenum Cofactor.Journal of the American Chemical Society · 2018Article
- Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase.Journal of visualized experiments : JoVE · 2017Article
- Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry.Chemical communications (Cambridge, England) · 2017Article
- Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.Journal of the American Chemical Society · 2017Article
- Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase.Journal of the American Chemical Society · 2017Article
- Vibrational Probes of Molybdenum Cofactor-Protein Interactions in Xanthine Dehydrogenase.Inorganic chemistry · 2017Article
- YedY: A Mononuclear Molybdenum Enzyme with a Redox-Active Ligand?Chembiochem : a European journal of chemical biology · 2016Article
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7 authors at 3 institutions in 3 countries.
Funding
Abstract
A long-standing contradiction in the field of mononuclear Mo enzyme research is that small-molecule chemistry on active-site mimic compounds predicts ligand participation in the electron transfer reactions, but biochemical measurements only suggest metal-centered catalytic electron transfer. With the simultaneous measurement of substrate turnover and reversible electron transfer that is provided by Fourier-transformed alternating-current voltammetry, we show that Escherichia coli YedY is a mononuclear Mo enzyme that reconciles this conflict. In YedY, addition of three protons and three electrons to the well-characterized "as-isolated" Mo(V) oxidation state is needed to initiate the catalytic reduction of either dimethyl sulfoxide or trimethylamine N-oxide. Based on comparison with earlier studies and our UV-vis redox titration data, we assign the reversible one-proton and one-electron reduction process centered around +174 mV vs. standard hydrogen electrode at pH 7 to a Mo(V)-to-Mo(IV) conversion but ascribe the two-proton and two-electron transition occurring at negative potential to the organic pyranopterin ligand system. We predict that a dihydro-to-tetrahydro transition is needed to generate the catalytically active state of the enzyme. This is a previously unidentified mechanism, suggested by the structural simplicity of YedY, a protein in which Mo is the only metal site.
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