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

Chemical Communications : Chem Comm
Woo Jae JeongWoon Ju Song

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.

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Citations

Mar 19, 2021·Organic & Biomolecular Chemistry·Andreas ThielJun Okuda
Apr 20, 2021·Journal of Inorganic Biochemistry·Daniel J DiPrimio, Patrick L Holland
May 4, 2021·Frontiers in Molecular Biosciences·Rafael Alcala-ToranoGiovanna Ghirlanda
Jun 1, 2021·ACS Catalysis·Sandro FischerAlexandria D Liang
Jun 10, 2021·The Journal of Physical Chemistry. B·Sergi RodaVictor Guallar
Aug 1, 2021·Journal of Inorganic Biochemistry·Se-Min JungWoon Ju Song
Oct 16, 2021·Biological Chemistry·Paul Ebensperger, Claudia Jessen-Trefzer

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Methods Mentioned

BETA
infrared
in silico methods
chemical modification
genetic modification

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