Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor

被引：1

作者：

Fernandez-Lopez, Laura ^{[1
]}

Cea-Rama, Isabel ^{[2
]}

Alvarez-Malmagro, Julia ^{[1
,5
]}

Ressmann, Anna K. ^{[3
]}

Gonzalez-Alfonso, Jose L. ^{[1
]}

Coscolin, Cristina ^{[1
]}

Shahgaldian, Patrick ^{[4
]}

Plou, Francisco J. ^{[1
]}

Modregger, Jan ^{[3
]}

Pita, Marcos ^{[1
]}

Sanz-Aparicio, Julia ^{[2
]}

Ferrer, Manuel ^{[1
]}

机构：

[1] CSIC, Inst Catalisis & Petroleoquim ICP, Madrid 28049, Spain

[2] CSIC, Inst Quim Fis Rocasolano IQFR, Madrid 28006, Spain

[3] Eucodis Biosci GMBH, A-1030 Vienna, Austria

[4] Univ Appl Sci & Arts Northwestern Switzerland, Inst Ecopreneurship, Sch Life Sci, CH-4132 Muttenz, Switzerland

[5] Univ Seville, Dept Phys Chem, Seville 41012, Spain

来源：

CHEMICAL COMMUNICATIONS | 2023年 / 59卷 / 62期

基金：

欧盟地平线“2020”;

关键词：

ARTIFICIAL METALLOENZYMES; ACTIVE-SITE; EVOLUTION; PROTEINS; DESIGN;

D O I：

10.1039/d3cc01946b

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Metal complexes introduced into protein scaffolds can generate versatile biomimetic catalysts endowed with a variety of catalytic properties. Here, we synthesized and covalently bound a bipyridinyl derivative to the active centre of an esterase to generate a biomimetic catalyst that shows catecholase activity and enantioselective catalytic oxidation of (+)-catechin.

引用

页码：9469 / 9472

页数：5

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