Issue 14, 2023

An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition

Abstract

We repurposed the metal-binding site of a cupin superfamily protein into the 2-His-1-carboxylate facial triad, which is one of the common motifs in natural non-heme enzymes, to construct artificial metalloenzymes that can catalyze new-to-nature reactions. The Cu2+-H52A/H58E variant catalyzed the stereoselective Michael addition reaction and was found to bear a flexible metal-binding site in the high-resolution crystal structure. Furthermore, the H52A/H58E/F104W mutant accommodated a water molecule, which was supported by Glu58 and Trp104 residues via hydrogen bonding, presumably leading to high stereoselectivity. Thus, the 2-His-1-carboxylate facial triad was confirmed to be a versatile and promising metal-binding motif for abiological and canonical biological reactions.

Graphical abstract: An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition

Supplementary files

Article information

Article type
Edge Article
Submitted
11 Dec 2022
Accepted
28 Feb 2023
First published
13 Mar 2023
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2023,14, 3932-3937

An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition

R. Matsumoto, S. Yoshioka, M. Yuasa, Y. Morita, G. Kurisu and N. Fujieda, Chem. Sci., 2023, 14, 3932 DOI: 10.1039/D2SC06809E

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements