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A De Novo Designed Metalloenzyme for the Hydration of CO2.

Authors :
Cangelosi, Virginia M.
Deb, Aniruddha
Penner-Hahn, James E.
Pecoraro, Vincent L.
Source :
Angewandte Chemie International Edition; Jul2014, Vol. 53 Issue 30, p7900-7903, 4p
Publication Year :
2014

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<superscript>II</superscript> metalloenzyme was prepared using de novo design. α<subscript>3</subscript>DH<subscript>3</subscript> folds into a stable single‐stranded three‐helix bundle and binds Zn<superscript>II</superscript> with high affinity using His<subscript>3</subscript>O coordination. The resulting metalloenzyme catalyzes the hydration of CO<subscript>2</subscript> 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
14337851
Volume :
53
Issue :
30
Database :
Complementary Index
Journal :
Angewandte Chemie International Edition
Publication Type :
Academic Journal
Accession number :
97119263
Full Text :
https://doi.org/10.1002/anie.201404925