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Incorporation of metal-chelating unnatural amino acids into halotag for allylic deamination


Stein, Alina; Liang, Alexandria Deliz; Sahin, Reyhan; Ward, Thomas R (2022). Incorporation of metal-chelating unnatural amino acids into halotag for allylic deamination. Journal of Organometallic Chemistry, 962:122272.

Abstract

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 [(η5-C5H5)Ru(MeCN)3]+.

Abstract

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 [(η5-C5H5)Ru(MeCN)3]+.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Life Sciences > Biochemistry
Physical Sciences > Physical and Theoretical Chemistry
Physical Sciences > Organic Chemistry
Physical Sciences > Inorganic Chemistry
Physical Sciences > Materials Chemistry
Uncontrolled Keywords:Materials Chemistry, Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Biochemistry
Language:English
Date:1 March 2022
Deposited On:09 Jan 2023 08:27
Last Modified:30 Jan 2024 02:37
Publisher:Elsevier
ISSN:0022-328X
OA Status:Hybrid
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1016/j.jorganchem.2022.122272
Project Information:
  • : FunderMarie Curie
  • : Grant IDH2020- MSCA-IF-2017
  • : Project Title
  • : FunderH2020
  • : Grant ID694424
  • : Project TitleDirected Evolution of Artificial Metalloenzymes for In Vivo Applications
  • : FunderSNSF
  • : Grant ID182046
  • : Project TitleDirected Evolution of Artificial Metalloproteins and Metalloenzymes
  • Content: Published Version
  • Licence: Creative Commons: Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)