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A De Novo Designed Metalloenzyme for the Hydration of CO 2
Author(s) -
Cangelosi Virginia M.,
Deb Aniruddha,
PennerHahn James E.,
Pecoraro Vincent L.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201404925
Subject(s) - carbonic anhydrase , chemistry , carbonic anhydrase ii , enzyme , helix bundle , catalysis , stereochemistry , gene isoform , helix (gastropod) , molecule , biochemistry , protein structure , organic chemistry , biology , gene , ecology , snail
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. α 3 DH 3 folds into a stable single‐stranded three‐helix bundle and binds Zn II with high affinity using His 3 O coordination. The resulting metalloenzyme catalyzes the hydration of CO 2 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.