Unknown

Dataset Information

0

Selective Enzymatic Oxidation of Silanes to Silanols.


ABSTRACT: 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 (P450BM3 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.

SUBMITTER: Bahr S 

PROVIDER: S-EPMC7511438 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC10222655 | biostudies-literature
| S-EPMC7027454 | biostudies-literature
| S-EPMC5798593 | biostudies-literature
| S-EPMC2509579 | biostudies-literature
| S-EPMC5257249 | biostudies-literature
| S-EPMC8675236 | biostudies-literature
| S-EPMC3062704 | biostudies-literature
| S-EPMC4281339 | biostudies-literature
| S-EPMC5770511 | biostudies-literature
| S-EPMC10019461 | biostudies-literature