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| - Quantitative Structure−Activity Relationship BasedQuantification of the Impacts of Enzyme−Substrate Bindingon Rates of Peroxidase-Mediated Reactions of EstrogenicPhenolic Chemicals
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| - The initial rates of horseradish peroxidase (HRP)-mediated enzymatic reactions of 15 assortedaqueous phase phenolic chemicals were studied. The associated reaction rate constants were found tocorrelate quantitatively with two independent variables: the highest-occupied molecular orbital energy(EHOMO) defining the intrinsic redox reactivities of the phenolic substrates and the distance between asubstrate and the δN of HIS42's imidazole ring in an HRP/substrate binding complex, obtained throughmolecular simulations. Highly correlated quantitative structure−activity relationship (QSAR) equations werethus developed. This work provides insights into the impacts that HRP/substrate binding may have onHRP-mediated reactions. Additionally, the QSAR equations developed in the work may serve as a basisto further explore the potential use of HRP-mediated reactions in the treatment of estrogenic contaminants,and they constitute an important tool for redesign and screening of potential proteomic modifications to thewild-type HRP structure intended to enhance reactivity toward selected substrates.
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