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A Hydroxyquinoline-Based Unnatural Amino Acid for the Design of Novel Artificial Metalloenzymes.


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, CuII , ZnII and RhIII to form unique artificial metalloenzymes. The catalytic potential of the CuII -bound LmrR_HQAla enzyme was shown through its ability to catalyse asymmetric Friedel-Craft alkylation and water addition, whereas the ZnII -coupled enzyme was shown to mimic natural Zn hydrolase activity.

SUBMITTER: Drienovska I 

PROVIDER: S-EPMC7689906 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

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A Hydroxyquinoline-Based Unnatural Amino Acid for the Design of Novel Artificial Metalloenzymes.

Drienovská Ivana I   Scheele Remkes A RA   Gutiérrez de Souza Cora C   Roelfes Gerard G  

Chembiochem : a European journal of chemical biology 20200717 21


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<sup>II</sup> , Zn<sup>II</sup> and Rh<sup>III</sup> to form unique artificial metalloenzymes. The catalyt  ...[more]

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