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Bioorthogonal Enzymatic Activation of Caged Compounds

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Acevedo-Rocha,  Carlos G.
Philipps-Universität Marburg, Fachbereich Chemie;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
LOEWE Zentrum Synthet Mikrobiol SYNMIKRO, D-35043 Marburg, Germany;
Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany;

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Lonsdale,  Richard
Philipps-Universität Marburg, Fachbereich Chemie;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Reetz,  Manfred T.
Philipps-Universität Marburg, Fachbereich Chemie;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Ritter, C., Nett, N., Acevedo-Rocha, C. G., Lonsdale, R., Kraling, K., Dempwolff, F., et al. (2015). Bioorthogonal Enzymatic Activation of Caged Compounds. Angewandte Chemie International Edition, 54(45), 13440-13443. doi:10.1002/anie.201506739.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-228F-2
Abstract
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.