ArticleApplied and environmental microbiology2008
Protein engineering of toluene monooxygenases for synthesis of chiral sulfoxides.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 47 citations in OpenAlex.
- Mutagenesis and expression of methane monooxygenase to alter regioselectivity with aromatic substrates.FEMS microbiology letters · 2017Article
- RNA-seq transcriptome analysis of a Pseudomonas strain with diversified catalytic properties growth under different culture medium.MicrobiologyOpen · 2016Article
- The Toluene o-Xylene Monooxygenase Enzymatic Activity for the Biosynthesis of Aromatic Antioxidants.PloS one · 2015Article
- Enantioselective imidation of sulfides via enzyme-catalyzed intermolecular nitrogen-atom transfer.Journal of the American Chemical Society · 2014Article
- Article
- Study of the TmoS/TmoT two-component system: towards the functional characterization of the family of TodS/TodT like systems.Microbial biotechnology · 2012Article
- Engineering non-heme mono- and dioxygenases for biocatalysis.Computational and structural biotechnology journal · 2012Review
- When second best is good enough: another probabilistic look at saturation mutagenesis.Applied and environmental microbiology · 2012Article
- Tuning the specificity of the recombinant multicomponent toluene o-xylene monooxygenase from Pseudomonas sp. strain OX1 for the biosynthesis of tyrosol from 2-phenylethanol.Applied and environmental microbiology · 2011Article
- Improving biocatalyst performance by integrating statistical methods into protein engineering.Applied and environmental microbiology · 2010Article
- Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate.Nature chemical biology · 2009Article
- HotSpot Wizard: a web server for identification of hot spots in protein engineering.Nucleic acids research · 2009Article
- Rapid methods for high-throughput detection of sulfoxides.Applied and environmental microbiology · 2009Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enantiopure sulfoxides are valuable asymmetric starting materials and are important chiral auxiliaries in organic synthesis. Toluene monooxygenases (TMOs) have been shown previously to catalyze regioselective hydroxylation of substituted benzenes and phenols. Here we show that TMOs are also capable of performing enantioselective oxidation reactions of aromatic sulfides. Mutagenesis of position V106 in the alpha-hydroxylase subunit of toluene ortho-monooxygenase (TOM) of Burkholderia cepacia G4 and the analogous position I100 in toluene 4-monooxygenase (T4MO) of Pseudomonas mendocina KR1 improved both rate and enantioselectivity. Variant TomA3 V106M of TOM oxidized methyl phenyl sulfide to the corresponding sulfoxide at a rate of 3.0 nmol/min/mg protein compared with 1.6 for the wild-type enzyme, and the enantiomeric excess (pro-S) increased from 51% for the wild type to 88% for this mutant. Similarly, T4MO variant TmoA I100G increased the wild-type oxidation rate by 1.7-fold, and the enantiomeric excess rose from 86% to 98% (pro-S). Both wild-type enzymes showed lower activity with methyl para-tolyl sulfide as a substrate, but the improvement in the activity and enantioselectivity of the mutants was more dramatic. For example, T4MO variant TmoA I100G oxidized methyl para-tolyl sulfide 11 times faster than the wild type did and changed the selectivity from 41% pro-R to 77% pro-S. A correlation between regioselectivity and enantioselectivity was shown for TMOs studied in this work. Using in silico homology modeling, it is shown that residue I100 in T4MO aids in steering the substrate into the active site at the end of the long entrance channel. It is further hypothesized that the main function of V106 in TOM is the proper positioning or docking of the substrate with respect to the diiron atoms. The results from this work suggest that when the substrate is not aligned correctly in the active site, the oxidation rate is decreased and enantioselectivity is impaired, resulting in products with both chiral configurations.
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