Sabine Brinkmann-Chen California Institute of Technology
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 make silanols. Directed evolution enhanced this non-native activity and created a highly efficient catalyst for selective silane oxidation under mild conditions with oxygen as terminal oxidant. The evolved enzyme does not touch C–H bonds also present in the silane substrates, nor does this biotransformation 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 P450’s native C–H hydroxylation mechanism. Enzymatic silane oxidation now extends Nature’s already impressive catalytic repertoire.
download asset 20200317_SiOx.pdf 0.82 MB [opens in a new tab] cloud_download
pdf : 0.82 MB
download asset 20200209_SI.pdf 2 MB [opens in a new tab] cloud_download
pdf : 2 MB