Electrostatic preactivation, a missing step in dioxygen activation
Abstract
Dioxygen is the oxidant of aerobic life, yet most closed-shell molecules are stable in its presence. 1–4 Conventional accounts of dioxygen activation begin with electron transfer to O 2 , typically from a redox-active metal centre or cofactor. 5–9 Here we show that preparing dioxygen to receive that electron is a separate function, discharged by the electrostatic environment alone, and that the two can be tuned independently. At the equilibrium geometry of neutral O 2 the anion that must receive the electron is unbound; 10,11 a Lewis-acidic field removes this obstacle before any charge moves, a stage we term preactivation . Point charges alone split the O 2 π* manifold and bind the anion at the neutral geometry. Reaction-path calculations show that inner-sphere electron transfer from the Zn–C bond, which generates a superoxide/alkyl-radical pair without metal-centred redox chemistry, is rate-determining. Calibrated on dialkylzincs alone, the in-plane anisotropy of the field gradient, with one term in the charge and distance of the metal resolved within the same series, predicts the π* splitting to within 7% in four enzyme active sites containing iron, copper, nickel or no metal. The electrostatic contribution of an enzyme active site to preactivation can thus be quantified on a scale calibrated with redox-silent organozinc compounds.
Related
- Dioxygen Reduction at a Cu(I) Complex Supported by a Macrocyclic N3O Ligand System
- Axial Ligand Tuning of the Catalytic Two- versus Four-Electron Reduction of Dioxygen by a Dinuclear Cobalt Complex.
- Polarization Is Required to Model Electrostatic Preorganization: The Case of Chorismate Mutase
- Ensemble Molecular Surface Electrostatic Potential Descriptors as Informative Features for Active Learning
- Short-Rotation Coppice Pellets as Biofuels in a Modern Boiler with an Electrostatic Precipitator: Particulate Matter and Carbon Monoxide Emissions
BibTeX
@misc{jedrzejczyk2026electrostatic,
title = {{Electrostatic preactivation, a missing step in dioxygen activation}},
author = {Grzegorz Jędrzejczyk and Janusz Lewiński},
howpublished = {ChemRxiv},
year = {2026},
month = oct,
doi = {10.26434/chemrxiv.15007775/v2},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15007775/v2},
note = {CC BY},
}
RIS
TY - UNPB
TI - Electrostatic preactivation, a missing step in dioxygen activation
AU - Grzegorz Jędrzejczyk
AU - Janusz Lewiński
PY - 2026
DA - 2026/10/13
PB - ChemRxiv
DO - 10.26434/chemrxiv.15007775/v2
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15007775/v2
AB - Dioxygen is the oxidant of aerobic life, yet most closed-shell molecules are stable in its presence. 1–4 Conventional accounts of dioxygen activation begin with electron transfer to O 2 , typically from a redox-active metal centre or cofactor. 5–9 Here we show that preparing dioxygen to receive that electron is a separate function, discharged by the electrostatic environment alone, and that the two can be tuned independently. At the equilibrium geometry of neutral O 2 the anion that must receive the electron is unbound; 10,11 a Lewis-acidic field removes this obstacle before any charge moves, a stage we term preactivation . Point charges alone split the O 2 π* manifold and bind the anion at the neutral geometry. Reaction-path calculations show that inner-sphere electron transfer from the Zn–C bond, which generates a superoxide/alkyl-radical pair without metal-centred redox chemistry, is rate-determining. Calibrated on dialkylzincs alone, the in-plane anisotropy of the field gradient, with one term in the charge and distance of the metal resolved within the same series, predicts the π* splitting to within 7% in four enzyme active sites containing iron, copper, nickel or no metal. The electrostatic contribution of an enzyme active site to preactivation can thus be quantified on a scale calibrated with redox-silent organozinc compounds.
ER -