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  • Title: A de novo designed metalloenzyme for the hydration of CO2.
    Author: Cangelosi VM, Deb A, Penner-Hahn JE, Pecoraro VL.
    Journal: Angew Chem Int Ed Engl; 2014 Jul 21; 53(30):7900-3. PubMed ID: 24943466.
    Abstract:
    Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature's approach to catalysis, a Zn(II) metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single-stranded three-helix bundle and binds Zn(II) with high affinity using His3 O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400-fold of the fastest carbonic anhydrase isoform, CAII, and 11-fold of CAIII.
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