Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase

Author:

Linde Dolores1234,Cañellas Marina56748,Coscolín Cristina1234,Davó-Siguero Irene1234,Romero Antonio1234,Lucas Fátima56748,Ruiz-Dueñas Francisco J.1234,Guallar Victor56749,Martínez Angel T.1234

Affiliation:

1. Centro de Investigaciones Biológicas

2. CSIC

3. E-28040 Madrid

4. Spain

5. Joint BSC-CRG-IRB Research Program in Computational Biology

6. Barcelona Supercomputing Center

7. E-08034 Barcelona

8. Anaxomics Biotech

9. ICREA

Abstract

By enlarging the active site of DyP, F359G stereoselectively converting methyl-phenyl sulfide (MPS) into S methyl-phenyl sulfoxide (MPSO) was obtained, while the parent DyP has no activity, and L357G yields racemic mixtures.

Publisher

Royal Society of Chemistry (RSC)

Subject

Catalysis

Reference50 articles.

1. Recent Developments in the Synthesis and Utilization of Chiral Sulfoxides

2. H. Gröger , in Catalytic Asymmetric Synthesis, ed. I. Ojima, John Wiley & Sons, Inc., 2010, pp. 269–341

3. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

4. Recent biotechnological developments in the use of peroxidases

5. A. Matura and K. H.van Pee, in Enzyme catalysis in organic synthesis: A comprehensive handbook, ed. K. Drautz, H. Gröger and O. May, Wiley, Weinheim, 2012, pp. 1553–1567

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