Enzymes may work like miniature particle accelerators by using intense electrical fields to rip electrons off molecules.
April 24, 2026
Original Paper
Field-Assisted Substrate Ionization as a Plausible Initiating Step in Enzyme Catalysis
ChemRxiv · chemrxiv.15002317/v1
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The Takeaway
High school biology teaches that enzymes speed up reactions by acting like a lock and key for specific molecules. This new theory suggests that enzymes actually generate massive internal electrostatic fields. These fields are strong enough to physically pull electrons away from their targets to kickstart chemical changes. This makes the enzyme more of an active electrical switch than a passive structural template. If true, this completely changes our understanding of how life's fundamental chemical reactions are controlled.
From the abstract
Enzymes are widely understood to accelerate chemical reactions through transition-state stabilization and optimizing the orientation of reactants within their active sites. A growing body of work highlights the central role of strong electrostatic fields in these processes with magnitudes reaching ~108–1010 V/m in enzyme active sites. Here, we explore the hypothesis that such fields may, in some cases, facilitate catalysis by inducing field-assisted electron transfer or partial ionization of bou