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A de?novo designed metalloenzyme for the hydration of CO2.

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. ?3DH3 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.

SUBMITTER: Cangelosi VM

PROVIDER: S-EPMC4107010 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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A de novo designed metalloenzyme for the hydration of CO2.

Cangelosi Virginia M VM Deb Aniruddha A Penner-Hahn James E JE Pecoraro Vincent L VL

Angewandte Chemie (International ed. in English) 20140618 30

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 ...[more]

PMID: 24943466

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