Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 45, Pages 13440-13443Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201506739
Keywords
bioorthogonal chemistry; directed evolution; cytochromes; protecting groups; protein engineering
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Funding
- LOEWE Research Cluster of the State of Hesse (SynChemBio)
- University of Marburg
- Max-Planck Society
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Engineered cytochromeP450 monooxygenase variants are reported as highly active and selective catalysts for the bioorthogonal uncaging of propargylic and benzylic ether protected substrates, including uncaging in living E. coli. observed selectivity is supported by induced-fit docking and molecular dynamics simulations. This proof-of-principle study points towards the utility of bioorthogonal enzyme/protecting group pairs for applications in the life sciences.
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