Wang et al. recently reported an in silico study of the trichodiene synthase (TDS) conversion of farnesyl diphosphate (FPP) to trichodiene (TD) (Wang et al., ACS Catal. 2017, 7, 5841-5846). Although the methods and level of theory used in that work are nearly identical to our own recent work on this system (Dixit et al., ACS Catal. 2017, 7, 812-818), Wang et al. reach rather different conclusions. The authors claimed to obtain a "very credible" mechanism for the biosynthesis of TD based on the optimized folding mode of FPP in the 1,6-ring closure in TDS. However, the folding mode of the FPP substrate that was presented contradicts NMR and mass spectrometry data. Moreover, the authors make numerous incorrect statements regarding our earlier work.
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This contribution has been supported by the Israel Science Foundation (Grant No. 2146/15), the National Institutes of Health (GM46736), and National Natural Science Foundation of China (Grant No. 21533003).
© 2017 American Chemical Society.