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 JournalArticleAcademicpeer-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, 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.

Original languageEnglish
Pages (from-to)3077-3081
JournalChemBioChem
Volume21
Issue number21
DOIs
Publication statusAccepted/In press - 1 Jan 2020

Keywords

  • biocatalysis
  • hybrid catalysts
  • metalloenzymes
  • noncanonical amino acids
  • protein design

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