ArticleInorganic chemistry2017
Vibrational Probes of Molybdenum Cofactor-Protein Interactions in Xanthine Dehydrogenase.
Article in Inorganic chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Molybdenum Cofactor Model Reveals Remarkable Redox Activity at Both Molybdenum and the Pyranopterin Dithiolene Ligand.Journal of the American Chemical Society · 2025Article
- Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis.Molecules (Basel, Switzerland) · 2023Review
- Resonance Raman spectroscopy of pyranopterin molybdenum enzymes.Journal of inorganic biochemistry · 2022Review
- Spectroscopic Studies of Mononuclear Molybdenum Enzyme Centers.Molecules (Basel, Switzerland) · 2022Review
- Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.Metal ions in life sciences · 2020Article
- Metal-Dithiolene Bonding Contributions to Pyranopterin Molybdenum Enzyme Reactivity.Inorganics · 2020Article
- Implications of Pyran Cyclization and Pterin Conformation on Oxidized Forms of the Molybdenum Cofactor.Journal of the American Chemical Society · 2018Article
- Xanthine oxidase-product complexes probe the importance of substrate/product orientation along the reaction coordinate.Dalton transactions (Cambridge, England : 2003) · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The pyranopterin dithiolene (PDT) ligand is an integral component of the molybdenum cofactor (Moco) found in all molybdoenzymes with the sole exception of nitrogenase. However, the roles of the PDT in catalysis are still unknown. The PDT is believed to be bound to the proteins by an extensive hydrogen-bonding network, and it has been suggested that these interactions may function to fine-tune Moco for electron- and atom-transfer reactivity in catalysis. Here, we use resonance Raman (rR) spectroscopy to probe Moco-protein interactions using heavy-atom congeners of lumazine, molecules that bind tightly to both wild-type xanthine dehydrogenase (wt-XDH) and its Q102G and Q197A variants following enzymatic hydroxylation to the corresponding violapterin product molecules. The resulting enzyme-product complexes possess intense near-IR absorption, allowing high-quality rR spectra to be collected on wt-XDH and the Q102G and Q197A variants. Small negative frequency shifts relative to wt-XDH are observed for the low-frequency Moco vibrations. These results are interpreted in the context of weak hydrogen-bonding and/or electrostatic interactions between Q102 and the -NH
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