Journal
JOURNAL OF ORGANOMETALLIC CHEMISTRY
Volume 962, Issue -, Pages -Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jorganchem.2022.122272
Keywords
HaloTag; Unnatural amino acid; Deallylation; Artificial metalloenzyme; Metal-chelating
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The potential of artificial metalloenzymes has increased interest in the design of novel metal-binding sites in proteins. Metal-chelating unnatural amino acids provide a promising solution for engineering active metal sites in a defined way. In this study, four metal-chelating unnatural amino acids were introduced into HaloTag, an attractive scaffold for assembling functional artificial metalloenzymes. By complementation with [(eta(5)-C5H5)Ru(MeCN)(3)](+), HaloTag engineered with 2-amino-3-(8-hydroxyquinolin-5-yl)propanoic acid (HQ-Ala-1) was used to assemble an artificial metalloenzyme for improved allylic deamination.
The potential of artificial metalloenzymes has led to an increase in interest for the design of novel metal-binding sites in proteins. Metal-chelating unnatural amino acids offer an auspicious solution to engineer active metal sites in a defined way. Herein, we describe the introduction of four metal-chelating unnatural amino acids into HaloTag, an attractive scaffold for the assembly of functional artificial metalloenzymes. HaloTag, engineered with 2-amino-3-(8-hydroxyquinolin-5-yl)propanoic acid (HQ-Ala-1) was used to assemble an artificial metalloenzyme for improved allylic deamination upon complementation with [(eta(5)-C5H5)Ru(MeCN)(3)](+). (C) 2022 The Authors. Published by Elsevier B.V.
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