Se site targeted-two circles antioxidant in GPx4-like catalytic peroxide degradation by polyphenols (-)-epigallocatechin gallate and genistein using SERS

Mengmeng Zhang; Jingbo Liu; Yu Gao; Bing Zhao; Meng-Lei Xu; Ting Zhang

doi:10.1016/j.fochx.2024.101387

Se site targeted-two circles antioxidant in GPx4-like catalytic peroxide degradation by polyphenols (-)-epigallocatechin gallate and genistein using SERS

Food Chem X. 2024 Apr 13:22:101387. doi: 10.1016/j.fochx.2024.101387. eCollection 2024 Jun 30.

Authors

Mengmeng Zhang¹, Jingbo Liu¹, Yu Gao², Bing Zhao³, Meng-Lei Xu^{1

3}, Ting Zhang¹

Affiliations

¹ Jilin Provincial Key Laboratory of Nutrition and Functional Food/ College of Food Science and Engineering, Jilin University, Changchun 130062, PR China.
² College of Plant Protection, Jilin Agricultural University, Changchun 130118, PR China.
³ State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, PR China.

Abstract

A Se site targeted-two circles antioxidant of polyphenols EGCG and genistein in glutathione peroxidase 4 (GPx4)-like catalytic peroxide H₂O₂ and cumene hydroperoxide degradation was demonstrated by surface-enhanced Raman scattering (SERS). Se atom's active center is presenting a 'low-oxidation' and a 'high-oxidation' catalytic cycle. The former is oxidized to selenenic acid (SeO^-) with a Raman bond at 619/ 610 cm^-1 assigned to the νO - Se by the hydroperoxide substrate at 544/ 551 cm^-1 assigned to ωHSeC decreased. Under oxidative stress, the enzyme shifted to 'high-oxidation' catalytic cycle, in which GPx4 shuttles between R-SeO^- and R-SeOO^- with a Raman intensity of bond at 840/ 860 cm^-1 assigned to νO[bond, double bond]Se. EGCG could act as a reducing agent both in H₂O₂ and Cu-OOH degradation, while, genistein can only reduce Cu-OOH, because it binds more readily to the selenium site in GPx4 than EGCG with a closer proximity, therefore may affect its simultaneous binding to coenzymes.

Keywords: (−)-epigallocatechin gallate; Antioxidant; Genistein; Glutathione peroxidase 4; Hydrogen bonding; Selenium site; Surface-enhanced Raman scattering.