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

被引:27
作者
Drienovska, Ivana [1 ]
Scheele, Remkes A. [1 ]
Gutierrez de Souza, Cora [1 ]
Roelfes, Gerard [1 ]
机构
[1] Univ Groningen, Stratingh Inst Chem, Nijenborgh 4, NL-9747 AG Groningen, Netherlands
基金
欧洲研究理事会;
关键词
biocatalysis; hybrid catalysts; metalloenzymes; noncanonical amino acids; protein design; GENETIC INCORPORATION; COMPUTATIONAL DESIGN; TERMINAL ALKYNES; PROTEIN; COMPLEXES; BINDING; DERIVATIVES; 8-HYDROXYQUINOLINE; METALLOPROTEIN; SITES;
D O I
10.1002/cbic.202000306
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3077 / 3081
页数:5
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