Data and Code for Asymmetric Enzymatic Hydrophosphorylation Through O2 Activation

Zhou, Y., Ge, Y., Harrison, W., Zhao, H. Nov. 9, 2026. “Input datasets and code for Asymmetric enzymatic hydrophosphorylation through O2 activation.” University of Illinois Urbana-Champaign. DOI: 10.13012/B2IDB-4996177_V1.

Zhou, Y., Ge, Y., Harrison, W., Zhao, H. Nov. 9, 2026. “ERP Spectra and Simulation Results for Asymmetric enzymatic hydrophosphorylation through O2 activation.” University of Illinois Urbana-Champaign. DOI: 10.13012/B2IDB-7697540_V1.

Zhou, Y., Ge, Y., Harrison, W., Zhao, H. Aug. 21, 2026. “Data for: Asymmetric enzymatic hydrophosphorylation via O₂ activation.” Dryad. Dataset. DOI: 10.5061/dryad.z34tmpgwg

Enzymatic carbon-phosphorus bond formation is extremely rare in nature, limiting biocatalytic access to phosphorus-containing compounds that are widely used in pharmaceuticals and agrochemicals. Here, we report an asymmetric enzymatic hydrophosphorylation through oxygen activation using a repurposed flavin-dependent enzyme. Mechanistic studies revealed that reactive oxygen species are converted into productive phosphorus-centered radicals, followed by radical addition and enzymatic hydrogen atom transfer, achieving high enantioselectivity. The enzyme accommodates diverse phosphorus-hydrogen donors that pose challenges to chemical catalysis, enabling the biosynthesis of valuable phosphorus-containing scaffolds. This work expands the scope of biocatalysis to programmable carbon-phosphorus bond formation and establishes a paradigm for channeling oxygen reactivity in enzymes.

Illinois Data Bank: screening and prediction tables, input data, and code

Illinois Data Bank: EPR spectra, spectra measurements, and simulations

Dryad: computational results