Selective Enzymatic Oxidation of Silanes to Silanols.

Susanne Bähr, Sabine Brinkmann-Chen, Marc Garcia-Borràs, John M Roberts, Dimitris E Katsoulis, K N Houk, Frances H Arnold

Angewandte Chemie (International ed. in English) 2020 Sep 01

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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 (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. © 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Citation

Susanne Bähr, Sabine Brinkmann-Chen, Marc Garcia-Borràs, John M Roberts, Dimitris E Katsoulis, K N Houk, Frances H Arnold. Selective Enzymatic Oxidation of Silanes to Silanols. Angewandte Chemie (International ed. in English). 2020 Sep 01;59(36):15507-15511