A De novo Designed Metalloenzyme for the Hydration of CO2

Overview

Journal Angew Chem Int Ed Engl

Specialty Chemistry

Date 2014 Jun 20

PMID 24943466

Citations 27

Authors

Virginia M Cangelosi

Aniruddha Deb

James E Penner-Hahn

Vincent L Pecoraro

Affiliations

Soon will be listed here.

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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