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Bioorthogonal Enzymatic Activation of Caged Compounds
Author(s) -
Ritter Cornelia,
Nett Nathalie,
AcevedoRocha Carlos G.,
Lonsdale Richard,
Kräling Katja,
Dempwolff Felix,
Hoebenreich Sabrina,
Graumann Peter L.,
Reetz Manfred T.,
Meggers Eric
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201506739
Subject(s) - bioorthogonal chemistry , chemistry , monooxygenase , combinatorial chemistry , enzyme , biocatalysis , cytochrome p450 , active site , catalysis , selectivity , cytochrome , biochemistry , stereochemistry , click chemistry , reaction mechanism
Engineered cytochrome P450 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.