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A Hydroxyquinoline‐Based Unnatural Amino Acid for the Design of Novel Artificial Metalloenzymes
Author(s) -
Drienovská Ivana,
Scheele Remkes A.,
Gutiérrez de Souza Cora,
Roelfes Gerard
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000306
Subject(s) - artificial enzyme , chemistry , chelation , combinatorial chemistry , enzyme , amino acid , catalysis , alkylation , biocatalysis , stereochemistry , hydrolase , metal ions in aqueous solution , metal , biochemistry , reaction mechanism , organic chemistry
Abstract We have examined the potential of the noncanonical amino acid (8‐hydroxyquinolin‐3‐yl)alanine (HQAla) for the design of artificial metalloenzymes. HQAla, a versatile chelator of late transition metals, was introduced into the lactococcal multidrug‐resistance regulator (LmrR) by stop codon suppression methodology. LmrR_HQAla was shown to complex efficiently with three different metal ions, Cu II , Zn II and Rh III to form unique artificial metalloenzymes. The catalytic potential of the Cu II ‐bound LmrR_HQAla enzyme was shown through its ability to catalyse asymmetric Friedel‐Craft alkylation and water addition, whereas the Zn II ‐coupled enzyme was shown to mimic natural Zn hydrolase activity.