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    Robust and Versatile Host Protein for the Design and Evaluation of Artificial Metal Centers

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    Type
    Article
    Authors
    Fischer, Johannes cc
    Renn, Dominik
    Quitterer, Felix
    Radhakrishnan, Anand
    Liu, Meina
    Makki, Arwa cc
    Ghoprade, Seema Arun cc
    Rueping, Magnus cc
    Arold, Stefan T. cc
    Groll, Michael cc
    Eppinger, Jörg cc
    KAUST Department
    Biological & Organometallic Catalysis Laboratories
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Chemical Engineering Program
    Chemical Science Program
    Computational Bioscience Research Center (CBRC)
    KAUST Catalysis Center (KCC)
    KAUST Catalysis Center (KCC), Division of Physical Sciences & Engineering and § Computational Bioscience Research Center (CBRC), Division of Biological Sciences & Engineering, King Abdullah University of Science and Technology (KAUST), 23955 Thuwal, MK, Saudi Arabia
    Office of the VP
    Physical Science and Engineering (PSE) Division
    Structural Biology and Engineering
    Date
    2019-11-12
    Embargo End Date
    2020-11-12
    Permanent link to this record
    http://hdl.handle.net/10754/660353
    
    Metadata
    Show full item record
    Abstract
    Artificial metalloenzymes (ArMs) have high potential in biotechnological applications as they combine the versatility of transition-metal catalysis with the substrate selectivity of enzymes. An ideal host protein should allow high-yield recombinant expression, display thermal and solvent stability to withstand harsh reaction conditions, lack nonspecific metal-binding residues, and contain a suitable cavity to accommodate the artificial metal site. Moreover, to allow its rational functionalization, the host should provide an intrinsic reporter for metal binding and structural changes, which should be readily amendable to high-resolution structural characterization. Herein, we present the design, characterization, and de novo functionalization of a fluorescent ArM scaffold, named mTFP*, that achieves these characteristics. Fluorescence measurements allowed direct assessment of the scaffold's structural integrity. Protein X-ray structures and transition metal Förster resonance energy transfer (tmFRET) studies validated the engineered metal coordination sites and provided insights into metal binding dynamics at the atomic level. The implemented active metal centers resulted in ArMs with efficient Diels-Alderase and Friedel-Crafts alkylase activities.
    Citation
    Fischer, J., Renn, D., Quitterer, F., Radhakrishnan, A., Liu, M., Makki, A., … Eppinger, J. (2019). Robust and Versatile Host Protein for the Design and Evaluation of Artificial Metal Centers. ACS Catalysis, 11371–11380. doi:10.1021/acscatal.9b02896
    Sponsors
    The staff of the Beamline X06SA at the Paul Scherrer Institute, SLS, Villigen, Switzerland, is acknowledged for assistance during data collection. The authors thank S. Abdul Rajjaka for help with the bioinformatic setup.
    Publisher
    American Chemical Society (ACS)
    Journal
    ACS Catalysis
    DOI
    10.1021/acscatal.9b02896
    Additional Links
    https://pubs.acs.org/doi/10.1021/acscatal.9b02896
    ae974a485f413a2113503eed53cd6c53
    10.1021/acscatal.9b02896
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program; Physical Science and Engineering (PSE) Division; Chemical Science Program; Chemical Engineering Program; KAUST Catalysis Center (KCC); Computational Bioscience Research Center (CBRC)

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