ArticleiScience2025
Mechanistic insights into the selective oxidation of D-arginine by the nonheme iron-dependent viomycin biosynthesis enzyme VioC.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Mechanistic Elucidation of BBOX-Catalyzed Hydroxylation and THP-Induced Oxidative Rearrangement via QM/MM Calculations.Molecules (Basel, Switzerland) · 2026Article
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Authors and funding
5 authors.
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Abstract
VioC, a nonheme iron enzyme, catalyzes different reactions with D- and L-arginine, hydroxylating L-arginine at C3 and oxidatively deaminating D-arginine. Combining molecular dynamics with quantum mechanics/molecular mechanics (QM/MM) simulations, we reveal that the chirality of D-arginine positions its C2-H bond in proximity to the Fe(IV)-oxo intermediate and optimizes the geometry for enhanced σ-orbital alignment, thereby guiding the initial hydrogen atom transfer (HAT) from C2. Subsequent reactivity favors HAT from the ammonium group over alternative Glu-mediated proton coupled electron transfer pathway, driving C2-N desaturation to form a cationic imine intermediate. Both the C2-hydroxylation and C2-C3 desaturation pathways were ruled out due to their higher energy barriers. The cationic imine intermediate then hydrolyzes to yield the final ketone product. These findings demonstrate how substrate stereochemistry controls reactive site accessibility, providing mechanistic understanding of reaction bifurcation in Fe/2OG-dependent oxygenases.
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