Computer-aided laccase engineering: toward biological oxidation of arylamines
| Autor: | M. Fátima Lucas, Felipe de Salas, Emanuele Monza, Gerard Santiago, Sandra Acebes, Ángel T. Martínez, Victor Guallar, Susana Camarero |
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| Přispěvatelé: | Barcelona Supercomputing Center, Ministerio de Economía y Competitividad (España) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
PELE
PANI Computer-aided design Oxidation--Measurement 010402 general chemistry Oxidació 01 natural sciences Redox QM/MM Arylamines Catalysis Enginyeria de proteïnes chemistry.chemical_compound Electron transfer Aniline Organic chemistry Enzyme kinetics Laccase 010405 organic chemistry Chemistry Enginyeria electrònica [Àrees temàtiques de la UPC] Substrate (chemistry) Proteins General Chemistry Combinatorial chemistry 0104 chemical sciences Protein engineering |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname Recercat. Dipósit de la Recerca de Catalunya UPCommons. Portal del coneixement obert de la UPC Universitat Politècnica de Catalunya (UPC) |
| Popis: | 10 p.-5 fig.-1 tab. Oxidation of arylamines, such as aniline, is of high industrial interest and laccases have been proposed as biocatalysts to replace harsh chemical oxidants. However, the reaction is hampered by the redox potential of the substrate at acid pH and enzyme engineering is required to improve the oxidation. In this work, instead of trying to improve the redox potential of the enzyme, we aim towards the (transient) substrate’s one and propose this as a more reliable strategy. We have successfully combined a computational approach with experimental validation to rationally design an improved biocatalyst. The in silico protocol combines classical and quantum mechanics to deliver atomic and electronic level detail on the two main processes involved: substrate binding and electron transfer. After mutant expression and comparison to the parent type, kinetic results show that the protocol accurately predicts aniline’s improved oxidation (2-fold kcat increase) in the engineered variant for biocatalyzed polyaniline production. This study was supported by the INDOX (KBBE-2013-7-613549) EU-project, and the NOESIS (BI0201456388-R) and OxiDesign (CTQ2013-48287-R) Spanish project. GS thanks an FPI grant of the Spanish Ministry of Competitiveness. |
| Databáze: | OpenAIRE |
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