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Directed evolution of hybrid enzymes: Evolving enantioselectivity of an achiral Rh-complex anchored to a protein

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/persons/resource/persons58919

Reetz,  M. T.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

/persons/resource/persons58885

Peyralans,  J. J.-P.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

/persons/resource/persons58787

Maichele,  A.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

/persons/resource/persons58557

Fu,  Y.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

/persons/resource/persons58812

Maywald,  M.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Reetz, M. T., Peyralans, J.-J.-P., Maichele, A., Fu, Y., & Maywald, M. (2006). Directed evolution of hybrid enzymes: Evolving enantioselectivity of an achiral Rh-complex anchored to a protein. Chemical Communications (Cambridge, U. K.), 4318-4320. doi:10.1039/b610461d.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-9397-A
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