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Bioorthogonal Enzymatic Activation of Caged Compounds
Authors:Cornelia Ritter  Nathalie Nett  Dr Carlos G Acevedo‐Rocha  Dr Richard Lonsdale  Katja Kräling  Dr Felix Dempwolff  Dr Sabrina Hoebenreich  Prof?Dr Peter L Graumann  Prof?Dr Manfred T Reetz  Prof?Dr Eric Meggers
Affiliation:1. Fachbereich Chemie, Philipps‐Universit?t Marburg, Hans‐Meerwein‐Stra?e 4, 35043 Marburg (Germany);2. Max‐Planck‐Institut für Kohlenforschung, Kaiser‐Wilhelm‐Platz 1, 45470 Mülheim an der Ruhr (Germany);3. LOEWE Zentrum für Synthetische Mikrobiologie (SYNMIKRO), Hans‐Meerwein‐Stra?e, 35043 Marburg (Germany);4. Max‐Planck‐Institut für terrestrische Mikrobiologie, Karl‐von‐Frisch‐Stra?e 10, 35043 Marburg (Germany);5. College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005 (P. R. China)
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.
Keywords:bioorthogonal chemistry  directed evolution  cytochromes  protecting groups  protein engineering
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