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Issue 67, 2020
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Proteins as diverse, efficient, and evolvable scaffolds for artificial metalloenzymes

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Abstract

By combining synthetic catalysts and biochemical tools, numerous artificial metalloenzymes have been designed to exhibit high catalytic activity and selectivity in diverse chemical transformations. Out of the nearly infinite number of discovered or characterised proteins, however, only a handful of proteins have been employed as scaffolds for artificial metalloenzymes, implying that specific proteins are preferred owing to their native structural, functional, or biochemical properties. In the present review, we extract and group the biochemical and structural properties of proteins that are advantageous in the design of artificial metalloenzymes; protein stability, pre-existing metal centre, native binding affinity for small molecules, confined and empty space, well-defined secondary structure, and native cellular location. The desirable properties highlight proteins as the key players in the design of metal-dependent biocatalysts. We also propose rarely considered, yet promising, proteins that could be versatile and unique scaffolds for novel metalloenzymes.

Graphical abstract: Proteins as diverse, efficient, and evolvable scaffolds for artificial metalloenzymes

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Article information


Submitted
30 Apr 2020
Accepted
13 Jul 2020
First published
21 Jul 2020

Chem. Commun., 2020,56, 9586-9599
Article type
Feature Article

Proteins as diverse, efficient, and evolvable scaffolds for artificial metalloenzymes

W. J. Jeong, J. Yu and W. J. Song, Chem. Commun., 2020, 56, 9586
DOI: 10.1039/D0CC03137B

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