Artificial metalloenzymes enabled by combining proteins with hemin via protein refolding

作     者：Jingping Ouyang Zhenfang Zhang RenéHübner Henrik Karring Changzhu Wu 欧阳敬平;张振方;RenéHübner;Henrik Karring;吴昌柱

作者机构：Department of PhysicsChemistry and PharmacyUniversity of Southern DenmarkCampusvej 555230 OdenseDenmark Helmholtz-Zentrum Dresden-RossendorfInstitute of Ion Beam Physics and Materials ResearchBautzner Landstrasse 40001328 DresdenGermany Department of Green TechnologyUniversity of Southern DenmarkCampusvej 555230 OdenseDenmark Danish Institute for Advanced Study(DIAS)University of Southern DenmarkCampusvej 555230 OdenseDenmark 

基　　金：the Independent Research Fund Denmark (DFF) through the Sapere Aude Leader Program the generous funding from the Novo Nordisk Foundation the Carlsberg Foundation for their support via the Semper Ardens (Accelerate) program the use of the HZDR Ion Beam Center TEM facilities and the funding of TEM Talos by the German Federal Ministry of Education and Research (BMBF) in the framework of HEMCP 

出 版 物：《Chinese Journal of Catalysis》 (催化学报(英文))

年 卷 期：2024年第67卷第12期

页      码：157-165页

摘      要：In this study,we unveil a conceptual technology for fabricating artificial metalloenzymes(ArMs)by deeply integrating hemin into protein scaffolds via a protein refolding process,a method that transcends the conventional scope of surface-level *** approach involves denaturing proteins,such as benzaldehyde lyase,green fluorescent protein,and Candida antarctica lipase B,to expose extensive reactive amino acid residues,which are then intricately linked with hemin using orthogonal click reactions,followed by protein *** process not only retains the proteins’structural integrity but expands proteins’*** most notable outcome of this methodology is the hemin@BAL variant,which demonstrated a remarkable 83.7%conversion rate in cyclopropanation reactions,far surpassing the capabilities of traditional hemin-based catalysis in *** success highlights the significant role of protein structure in the ArMs’activity and marks a substantial leap forward in chemical modification of *** findings suggest vast potentials of protein refolding approaches for ArMs across various catalytic applications,paving the way for future advancements in synthetic biology and synthetic chemistry.

主 题 词：Artificial metalloenzyme Protein denaturation Click reaction Protein refolding Hemin 

学科分类：081704[081704] 07[理学] 08[工学] 0817[工学-轻工类] 070303[070303] 0703[理学-化学类] 

核心收录：

D　O　I：10.1016/S1872-2067(24)60150-6

馆 藏 号：203155653...