Issue 13, 2021

Chemogenetic engineering of nitrobindin toward an artificial epoxygenase

Abstract

Chemogenetic engineering of metalloproteins emerges as a powerful strategy to generate proteins that catalyze non-natural reactions or convert non-natural substrates. Here, we report on an artificial metalloenzyme (ArM) based on the β-barrel protein nitrobindin (NB) equipped with a manganese protoporphyrin IX catalyst (MnPPIX@NB) for the epoxidation of aromatic alkenes. After exchanging the metal cofactor and two rounds of directed evolution, our ArM shows improved activity (>7-fold increase) with an ee of 20%. The evolution campaign also revealed the importance of the proximal ligand for peroxide activation and subsequent oxygen atom transfer. By utilizing cell adhesion-promoting peptides, a facile strategy is presented to immobilize ArMs on the surface of E. coli cells for on-cell catalysis and chemogenetic engineering of ArMs.

Graphical abstract: Chemogenetic engineering of nitrobindin toward an artificial epoxygenase

Supplementary files

Article information

Article type
Paper
Submitted
07 Apr 2021
Accepted
16 May 2021
First published
17 May 2021

Catal. Sci. Technol., 2021,11, 4491-4499

Chemogenetic engineering of nitrobindin toward an artificial epoxygenase

D. F. Sauer, M. Wittwer, U. Markel, A. Minges, M. Spiertz, J. Schiffels, M. D. Davari, G. Groth, J. Okuda and U. Schwaneberg, Catal. Sci. Technol., 2021, 11, 4491 DOI: 10.1039/D1CY00609F

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