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 |
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Pages (from-to) | 3077-3081 |
Number of pages | 6 |
Journal | ChemBioChem |
Issue number | 21 |
DOIs | |
Publication status | E-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