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

IF 7.1 Q1 ENGINEERING, CHEMICAL Chemical Engineering Journal Advances Pub Date : 2025-05-01 Epub 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

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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.

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通过新型二酮衍生物实现高效光酶偶联，扩大酶的作用范围

本研究提出了一种新的可见光响应二酮衍生物，3 -对苯二甲酸偶氮乙酰丙酮（BDC - AA），旨在提高真菌漆酶（EC 1.10.3.2）的催化活性。实验结果表明，BDC - AA特异性地结合到漆酶的底物结合袋上，使电子从分子的光激发态有效地转移到酶的T1Cu中心。这种相互作用在可见光照射下显著促进了非原生底物乙二胺四乙酸（EDTA）的氧化。分子对接、荧光猝灭和圆二色性分析揭示了BDC - aa -漆酶复合物的结构基础，证实了其稳定性和增强的电子传递效率。该组合系统无需额外的牺牲剂或辅助因子，突出了绿色生物催化和环境修复应用的有前途的途径。

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