Achieving efficient photo-enzyme coupling via a novel diketone derivative to expand the scope of enzyme action

IF 5.5 Q1 ENGINEERING, CHEMICAL

Chemical Engineering Journal Advances Pub Date : 2025-03-15 DOI:10.1016/j.ceja.2025.100732

Wentao Zhang , Shuyu Zhou , Hao Dong , Yifan Yu , Degui Gao , Yue Zhao , Wenguang Huang , Wei Liu , Hui Cheng , Lele Peng , Bingdang Wu

{"title":"Achieving efficient photo-enzyme coupling via a novel diketone derivative to expand the scope of enzyme action","authors":"Wentao Zhang , Shuyu Zhou , Hao Dong , Yifan Yu , Degui Gao , Yue Zhao , Wenguang Huang , Wei Liu , Hui Cheng , Lele Peng , Bingdang Wu","doi":"10.1016/j.ceja.2025.100732","DOIUrl":null,"url":null,"abstract":"<div><div>This study presents a novel visible light‑responsive diketone derivative, 3‑terphthalic acid azoacetylacetone (BDC‑AA), designed to extend fungal laccase (EC 1.10.3.2) catalytic activity. Experimental results show that BDC‑AA binds specifically to laccase's substrate binding pocket, enabling efficient electron transfer from the molecule's photoexcited state to the enzyme's T1Cu center. This interaction significantly promotes the oxidation of otherwise non‑native substrates, ethylenediaminetetraacetic acid (EDTA) under visible light irradiation. Molecular docking, fluorescence quenching, and circular dichroism analyses reveal the structural basis of the BDC‑AA–laccase complex, confirming the stability and enhanced electron transfer efficiency. The combined system operates without additional sacrificial agents or cofactors, highlighting a promising avenue for green biocatalysis and environmental remediation applications.</div></div>","PeriodicalId":9749,"journal":{"name":"Chemical Engineering Journal Advances","volume":"22 ","pages":"Article 100732"},"PeriodicalIF":5.5000,"publicationDate":"2025-03-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemical Engineering Journal Advances","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2666821125000298","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ENGINEERING, CHEMICAL","Score":null,"Total":0}

引用次数: 0

Abstract

This study presents a novel visible light‑responsive diketone derivative, 3‑terphthalic acid azoacetylacetone (BDC‑AA), designed to extend fungal laccase (EC 1.10.3.2) catalytic activity. Experimental results show that BDC‑AA binds specifically to laccase's substrate binding pocket, enabling efficient electron transfer from the molecule's photoexcited state to the enzyme's T1Cu center. This interaction significantly promotes the oxidation of otherwise non‑native substrates, ethylenediaminetetraacetic acid (EDTA) under visible light irradiation. Molecular docking, fluorescence quenching, and circular dichroism analyses reveal the structural basis of the BDC‑AA–laccase complex, confirming the stability and enhanced electron transfer efficiency. The combined system operates without additional sacrificial agents or cofactors, highlighting a promising avenue for green biocatalysis and environmental remediation applications.

Abstract Image