Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor-Reference-Cited by-同舟云学术

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

Published:2023 Issue:62 Volume:59 Page:9469-9472
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Fernandez-Lopez Laura¹^ORCID,Cea-Rama Isabel²^ORCID,Alvarez-Malmagro Julia¹^ORCID,Ressmann Anna K.³^ORCID,Gonzalez-Alfonso Jose L.¹^ORCID,Coscolín Cristina¹^ORCID,Shahgaldian Patrick⁴^ORCID,Plou Francisco J.¹^ORCID,Modregger Jan³^ORCID,Pita Marcos¹^ORCID,Sanz-Aparicio Julia²^ORCID,Ferrer Manuel¹^ORCID

Affiliation:

1. Instituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid 28049, Spain

2. Instituto de Quimica Fisica Rocasolano (IQFR), CSIC, Madrid 28006, Spain

3. Eucodis Bioscience GMBH, Wien 1030, Austria

4. Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Muttenz 4132, Switzerland

Abstract

Metal complexes introduced into esterase enzyme scaffolds can generate versatile biomimetic catalysts endowed with oxidoreductase activity.

Funder

Agencia Estatal de Investigación

H2020 Food

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CC/D3CC01946B

Reference26 articles.

1. Artificial Metalloenzymes: Challenges and Opportunities

2. Rational Design of a Functional Metalloenzyme: Introduction of a Site for Manganese Binding and Oxidation into a Heme Peroxidase

3. Catalysis by a De Novo Zinc-Mediated Protein Interface: Implications for Natural Enzyme Evolution and Rational Enzyme Engineering

4. Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site

5. Influence of Active Site Location on Catalytic Activity in de Novo-Designed Zinc Metalloenzymes

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