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

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)3077-3081
Number of pages6
JournalChemBioChem
Issue number21
DOIs
Publication statusE-pub ahead of print - 25-Jun-2020

Keywords

  • biocatalysis
  • hybrid catalysts
  • metalloenzymes
  • noncanonical amino acids
  • protein design
  • GENETIC INCORPORATION
  • COMPUTATIONAL DESIGN
  • TERMINAL ALKYNES
  • PROTEIN
  • COMPLEXES
  • BINDING
  • DERIVATIVES
  • 8-HYDROXYQUINOLINE
  • METALLOPROTEIN
  • SITES

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