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  • 2019 2000_4_merged_1572609726

    Accepted author manuscript, 16 MB, PDF document

    Embargo ends: 16/06/20

  • 2019 Nature Catal-paper1 (002)

    Final published version, 4 MB, PDF document

DOI

  • Sandra Alonso
    Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid
  • Gerard Santiago
    Barcelona Supercomputing Center (BSC),
  • Isabel Cea-Rama
    CSIC, Institute of Catalysis, Madrid, Spain.
  • Laura Fernandez-Lopez
    Institute of Catalysis, Madrid, Spain
  • Cristina Coscolín
    Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid
  • Jan Modregger
    EUCODIS Bioscience
  • Anna K. Ressmann
    EUCODIS Bioscience
  • Monica Martinez-Martinez
    Institute of Catalysis, Madrid, Spain
  • Helena Marrero
    Institute of Catalysis, Madrid, Spain
  • Rafael Bargiela
  • Marcos Pita
    Institute of Catalysis, Madrid, Spain
  • Jose L. Gonzalez-Alfonso
    Institute of Catalysis, Madrid, Spain
  • Manon L. Briand
    University of Applied Sciences and Arts Northwestern Switzerland
  • David Rojo
    Universidad CEU San Pablo, Madrid, Spain
  • Coral Barbas
    Universidad CEU San Pablo, Madrid, Spain
  • Francisco J Plou
    Institute of Catalysis, Madrid, Spain
  • Peter Golyshin
  • Patrick Shahgaldian
    University of Applied Sciences and Arts Northwestern Switzerland
  • Julia Sanz-Aparicio
    nstitute of Physical Chemistry Rocasolano, CSIC
  • Víctor Guallar
    Barcelona Supercomputing Center (BSC),
  • Manuel Ferrer
    Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid
Enzyme engineering has allowed not only the de novo creation of active sites catalysing known biological reactions with rates close to diffusion limits, but also the generation of abiological sites performing new-to-nature reactions. However, the catalytic advantages of engineering multiple active sites into a single protein scaffold are yet to be established. Here, we report on proteins with two active sites of biological and/or abiological origin, for improved natural and non-natural catalysis. The approach increased the catalytic properties, such as enzyme efficiency, substrate scope, stereoselectivity and optimal temperature window, of an esterase containing two biological sites. Then, one of the active sites was metamorphosed into a metal-complex chemocatalytic site for oxidation and Friedel–Crafts alkylation reactions, facilitating synergistic chemo- and biocatalysis in a single protein. The transformations of 1-naphthyl acetate into 1,4-naphthoquinone (conversion approx. 100%) and vinyl crotonate and benzene into 3-phenylbutyric acid (≥83%; e.e. >99.9%) were achieved in one pot with this artificial multifunctional metalloenzyme.
Original languageEnglish
JournalNature Catalysis
Early online date16 Dec 2019
DOIs
Publication statusE-pub ahead of print - 16 Dec 2019
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