Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 36, Pages 15507-15511Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202002861
Keywords
biocatalysis; directed evolution; monooxygenation; P450 enzymes; silanols
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Funding
- Dow University Partnership Initiative [227027AO]
- Rothenberg Innovation Initiative (RI2) Program
- NIH National Institute for General Medical Sciences [GM-124480]
- Deutsche Forschungsgemeinschaft (DFG) Postdoctoral Fellowship [BA 6604/1-1]
- Spanish MINECO [IJCI-2017-33411]
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Compared to the biological world's rich chemistry for functionalizing carbon, enzymatic transformations of the heavier homologue silicon are rare. We report that a wild-type cytochrome P450 monooxygenase (P450(BM3) from Bacillus megaterium, CYP102A1) has promiscuous activity for oxidation of hydrosilanes to give silanols. Directed evolution was applied to enhance this non-native activity and create a highly efficient catalyst for selective silane oxidation under mild conditions with oxygen as the terminal oxidant. The evolved enzyme leaves C-H bonds present in the silane substrates untouched, and this biotransformation does not lead to disiloxane formation, a common problem in silanol syntheses. Computational studies reveal that catalysis proceeds through hydrogen atom abstraction followed by radical rebound, as observed in the native C-H hydroxylation mechanism of the P450 enzyme. This enzymatic silane oxidation extends nature's impressive catalytic repertoire.
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