ArticleDalton transactions (Cambridge, England : 2003)2017
Xanthine oxidase-product complexes probe the importance of substrate/product orientation along the reaction coordinate.
Article in Dalton transactions (Cambridge, England : 2003), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- 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
- Mechanism of Antioxidant Activity of Betanin, Betanidin and Respective C15-Epimers via Shape Theory, Molecular Dynamics, Density Functional Theory and Infrared Spectroscopy.Molecules (Basel, Switzerland) · 2022Article
- 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
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A combination of reaction coordinate computations, resonance Raman spectroscopy, spectroscopic computations, and hydrogen bonding investigations have been used to understand the importance of substrate orientation along the xanthine oxidase reaction coordinate. Specifically, 4-thiolumazine and 2,4-dithiolumazine have been used as reducing substrates for xanthine oxidase to form stable enzyme-product charge transfer complexes suitable for spectroscopic study. Laser excitation into the near-infrared molybdenum-to-product charge transfer band produces rR enhancement patterns in the high frequency in-plane stretching region that directly probe the nature of this MLCT transition and provide insight into the effects of electron redistribution along the reaction coordinate between the transition state and the stable enzyme-product intermediate, including the role of the covalent Mo-O-C linkage in facilitating this process. The results clearly show that specific Mo-substrate orientations allow for enhanced electronic coupling and facilitate strong hydrogen bonding interactions with amino acid residues in the substrate binding pocket.
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