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Catalysts 2019, 9(4), 356; https://doi.org/10.3390/catal9040356

Tailoring a Soluble Diiron Monooxygenase for Synthesis of Aromatic N-oxides

1
Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekio 7, LT-10257 Vilnius, Lithuania
2
Department of Xenobiotics Biochemistry, Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekio 7,LT-10257 Vilnius, Lithuania
*
Author to whom correspondence should be addressed.
Received: 18 March 2019 / Revised: 3 April 2019 / Accepted: 3 April 2019 / Published: 12 April 2019
(This article belongs to the Special Issue Biocatalysts: Design and Application)
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Abstract

The aromatic N-oxides have received increased attention over the last few years due to their potential application in medicine, agriculture and organic chemistry. As a green alternative in their synthesis, the biocatalytic method employing whole cells of Escherichia coli bearing phenol monooxygenase like protein PmlABCDEF (from here on – PML monooxygenase) has been introduced. In this work, site-directed mutagenesis was used to study the contributions of active site neighboring residues I106, A113, G109, F181, F200, F209 to the regiospecificity of N-oxidation. Based on chromogenic indole oxidation screening, a collection of PML mutants with altered catalytic properties was created. Among the tested mutants, the A113G variant acquired the most distinguishable N-oxidations capacity. This new variant of PML was able to produce dioxides (quinoxaline-1,4-dioxide, 2,5-dimethylpyrazine-1,4-dioxide) and specific mono-N-oxides (2,3,5-trimethylpyrazine-1-oxide) that were unachievable using the wild type PML. This mutant also featured reshaped regioselectivity as N-oxidation shifted towards quinazoline-1-oxide compared to quinazoline-3-oxide that is produced by the wild type PML. View Full-Text
Keywords: soluble diiron monooxygenase; aromatic N-oxides; protein engineering; biocatalysis; mutagenesis soluble diiron monooxygenase; aromatic N-oxides; protein engineering; biocatalysis; mutagenesis
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Petkevičius, V.; Vaitekūnas, J.; Vaitkus, D.; Čėnas, N.; Meškys, R. Tailoring a Soluble Diiron Monooxygenase for Synthesis of Aromatic N-oxides. Catalysts 2019, 9, 356.

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