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An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein
Author(s) -
Podtetenieff John,
Taglieber Andreas,
Bill Eckhard,
Reijerse Edward J.,
Reetz Manfred T.
Publication year - 2010
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.201002106
Subject(s) - mutagenesis , chemistry , enantioselective synthesis , binding site , protein engineering , site directed mutagenesis , protein design , directed evolution , computational biology , combinatorial chemistry , stereochemistry , biochemistry , computer science , protein structure , biology , enzyme , mutation , catalysis , mutant , gene
Guided by nature : A designed binding site comprising the His/His/Asp motif for Cu II complexation has been constructed in a robust protein by site‐specific mutagenesis (see picture). The artificial metalloenzyme catalyzes an enantioselective Diels–Alder reaction.