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

Ivana Drienovská; Remkes A. Scheele; Cora Gutiérrez de Souza; Gerard Roelfes

doi:10.1002/cbic.202000306

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

Ivana Drienovská, Remkes A. Scheele, Cora Gutiérrez de Souza, Gerard Roelfes^*

^*Corresponding author for this work

Research output: Contribution to Journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	3077-3081
Number of pages	5
Journal	ChemBioChem
Volume	21
Issue number	21
Early online date	25 Jun 2020
DOIs	https://doi.org/10.1002/cbic.202000306
Publication status	Published - 2 Nov 2020

Keywords

biocatalysis
hybrid catalysts
metalloenzymes
noncanonical amino acids
protein design

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/cbic.202000306

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title = "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.",

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AU - Roelfes, Gerard

PY - 2020/11/2

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KW - protein design

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

Abstract

Keywords

UN SDGs

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