Chemically modulating monoamine neurotransmitter serotonin undergoes a physiological reaction of enzyme intermediated peroxidation to reconstruct dimeric self-assembled complex. A standard bivalent ligand approach dimeric serotonin increases structural and functional scaffolding with recognition-binding sites that are fundamentally more friendly than monovalent binding sites. Dimerization reaction accelerates the catalytic activity of one-electron oxidation at the C(4) position of serotonin to generate dual phenolic radicals in the presence of horseradish (HRP) and hydrogen peroxide (HO).
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