A De Novo Designed Metalloenzyme for the Hydration of CO21. (18th June 2014)

• Record Type: Journal Article
• Authors: Cangelosi, Virginia M.; Deb, Aniruddha; Penner‐Hahn, James E.; Pecoraro, Vincent L.
• Is Part Of: Angewandte Chemie. Volume 126:Number 30(2014)
• Page Start: 8034
• Page End: 8037
• Publication Date: 2014-06-18
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201404925
• Languages: English
• ISSNs: 0044-8249

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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 His₃O 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.</p> </abstract>