Promethazine Oxidation by Redox Mediation in Peroxidase Reactions

doi:10.1006/abbi.2000.1710

Archives of Biochemistry and Biophysics

Volume 380, Issue 2, 15 August 2000, Pages 251-256

https://doi.org/10.1006/abbi.2000.1710 Get rights and content

Abstract

The effect of promethazine on peroxidase-catalyzed oxidation of 3,3′,5,5′-tetramethylbenzidine was investigated at pH 5.4. Promethazine dose dependently introduced a lag in the appearance of tetramethylbenzidine charge-transfer complex monitored at 652 nm. Increasing concentrations of tetramethylbenzidine however decreased the lag period proportional to the tetramethylbenzidine concentration. Addition of promethazine to preformed charge transfer complex caused rapid bleaching of the blue-colored complex. Titration of promethazine with the yellow-colored diimine gave rise to the blue charge-transfer complex and the complete reduction of the species to the colorless parent amine compound. The available evidence suggests that promethazine is oxidized via redox mediation by tetramethylbenzidine peroxidase-oxidized products.

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Citation Excerpt :
Redox mediators can improve the catalytic performance of redox enzymes by promoting the transfer of electrons or hydrogen atoms in the redox process (Liu et al., 2021b). A previous study showed that HRP used 3,3′,5,5′-tetramethylbenzidine as a redox mediator to oxidize promethazine (Olorunniji et al., 2000). 1,4-polyisoprenes could be oxidized and degraded by HRP coupled with 1-hydroxybenzotriazole (Enoki et al., 2003).
The catalysis of HRP coupling with redox mediator was a feasible technology for the transformation of antibiotics. This work screened three effective redox mediators syringaldehyde (SYR), acetosyringone (AS) and p-coumaric acid (PCA) for the norfloxacin (NOR) transformation in HRP/redox mediator system. Then, compared their transformation characteristics under varying conditions. The molecular docking results indicated HRP catalytic mediator was spontaneous, and the absolute value order of free energy between three redox mediators and HRP was consistent with the order of NOR removal in experiment. The presence of humic acid (HA) and polystyrene (PS) microplastics could block the removal of NOR, and the inhibition effect was proportional to the level of HA and PS particles. Seven and six possible intermediate products were identified by using SYR/AS and PCA as redox mediators, respectively, and potential NOR transformation pathways were proposed. SYR and AS treatment had the same transformation products and pathways due to their similar structure, including defluorination, oxidation, cross-coupled with mediator, demethylation and dehydrogenation. While for the PCA group, NOR not only performed the above action (except defluorination), but also underwent decarbonylation. These findings may expand our knowledge of the conversion and fate of fluoroquinolones through HRP coupled with redox mediator in the environment.
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However, some drawbacks such as slow degradation rate and poor degradation efficiency limited the widespread application of HRP/H2O2 system. In order to solve the inherent problems of HRP/H2O2 system, the research on enhancing the degradation of organic pollutants by adding electron shuttle had attracted increasing attention (Chen et al., 2014; Liu et al., 2021; Saladino et al., 2013; Ximenes et al., 2008; Enoki et al., 2003; Olorunniji et al., 2000). Some electron shuttle such as chlorpromazine and 1-hydroxybenzotriazole had been used to strengthen the HRP/H2O2 system, but these added enhancers would be decomposed along with the degradation of pollutants (Saladino et al., 2013; Ximenes et al., 2008).
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Regular ArticlePromethazine Oxidation by Redox Mediation in Peroxidase Reactions

Abstract

Coord. Chem. Rev.

Arch. Biochem. Biophys.

Arch. Biochem. Biophys.

Anal. Biochem.

J. Biol. Chem.

Biochim. Biophys. Acta

Free. Radicals Biol. Med.

Anal. Biochem.

Adv. Inorg. Biochem.

Biochemistry

Regular Article
Promethazine Oxidation by Redox Mediation in Peroxidase Reactions