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 language | English |
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Pages (from-to) | 3077-3081 |
Number of pages | 5 |
Journal | ChemBioChem |
Volume | 21 |
Issue number | 21 |
Early online date | 25 Jun 2020 |
DOIs | |
Publication status | Published - 2 Nov 2020 |
Keywords
- biocatalysis
- hybrid catalysts
- metalloenzymes
- noncanonical amino acids
- protein design