ArticleMetal ions in life sciences2020
Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.
Article in Metal ions in life sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026Review
- Proton-Coupled OAT Triggers C2H2 Activation in a Bioinspired Molybdenum Complex.Journal of the American Chemical Society · 2026Article
- Active Site Structure and Mechanism of a Molybdenum Catechol Dehydroxylase.Journal of the American Chemical Society · 2026Article
- Molybdenum Cofactor Model Reveals Remarkable Redox Activity at Both Molybdenum and the Pyranopterin Dithiolene Ligand.Journal of the American Chemical Society · 2025Article
- Bond Valence Sum Parameters for Analyzing Pyranopterin Tungsten Enzyme Structures.Molecules (Basel, Switzerland) · 2025Article
- Second-Coordination-Sphere Effects Reveal Electronic Structure Differences between the Mitochondrial Amidoxime Reducing Component and Sulfite Oxidase.Inorganic chemistry · 2024Article
- Active Site Characterization of aInorganic chemistry · 2024Article
- Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis.Molecules (Basel, Switzerland) · 2023Review
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Resonance Raman spectroscopy of pyranopterin molybdenum enzymes.Journal of inorganic biochemistry · 2022Review
- Protonation and Non-Innocent Ligand Behavior in Pyranopterin Dithiolene Molybdenum Complexes.Inorganic chemistry · 2022Article
- Is There a Connection between the Metabolism of Copper, Sulfur, and Molybdenum in Alzheimer's Disease? New Insights on Disease Etiology.International journal of molecular sciences · 2022Review
- The Biochemical Landscape of Riboswitch Ligands.Biochemistry · 2022Article
- Active site architecture reveals coordination sphere flexibility and specificity determinants in a group of closely related molybdoenzymes.The Journal of biological chemistryArticle
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2 authors.
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Abstract
The last 20 years have seen a dramatic increase in our mechanistic understanding of the reactions catalyzed by pyranopterin Mo and W enzymes. These enzymes possess a unique cofactor (Moco) that contains a novel ligand in bioinorganic chemistry, the pyranopterin ene-1,2-dithiolate. A synopsis of Moco biosynthesis and structure is presented, along with our current understanding of the role Moco plays in enzymatic catalysis. Oxygen atom transfer (OAT) reactivity is discussed in terms of breaking strong metal-oxo bonds and the mechanism of OAT catalyzed by enzymes of the sulfite oxidase (SO) family that possess dioxo Mo(VI) active sites. OAT reactivity is also discussed in members of the dimethyl sulfoxide (DMSO) reductase family, which possess des-oxo Mo(IV) sites. Finally, we reveal what is known about hydride transfer reactivity in xanthine oxidase (XO) family enzymes and the formate dehydrogenases. The formal hydride transfer reactivity catalyzed by xanthine oxidase family enzymes is complex and cleaves substrate C-H bonds using a mechanism that is distinct from monooxygenases. The chapter primarily highlights developments in the field that have occurred since ~2000, which have contributed to our collective structural and mechanistic understanding of the three canonical pyranopterin Mo enzymes families: XO, SO, and DMSO reductase.
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