A Hydroxyquinoline‐Based Unnatural Amino Acid for the Design of Novel Artificial Metalloenzymes
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- Ivana Drienovská
- Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
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- Remkes A. Scheele
- Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
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- Cora Gutiérrez de Souza
- Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
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- Gerard Roelfes
- Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
書誌事項
- 公開日
- 2020-07-17
- 権利情報
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- http://creativecommons.org/licenses/by/4.0/
- DOI
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- 10.1002/cbic.202000306
- 公開者
- Wiley
この論文をさがす
説明
<jats:title>Abstract</jats:title><jats:p>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<jats:sup>II</jats:sup>, Zn<jats:sup>II</jats:sup> and Rh<jats:sup>III</jats:sup> to form unique artificial metalloenzymes. The catalytic potential of the Cu<jats:sup>II</jats:sup>‐bound LmrR_HQAla enzyme was shown through its ability to catalyse asymmetric Friedel‐Craft alkylation and water addition, whereas the Zn<jats:sup>II</jats:sup>‐coupled enzyme was shown to mimic natural Zn hydrolase activity.</jats:p>
収録刊行物
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- ChemBioChem
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ChemBioChem 21 (21), 3077-3081, 2020-07-17
Wiley