Sequential, all-bioorthogonal reaction cascade catalyzed by a dual functional artificial metalloenzyme inside encapsulin

22 June 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Spatial control over chemical reactions is a ubiquitous feature shared by all living organisms. In the present article, we describe the design of a proteinaceous, synthetic capsid based on the well-described bacterial nanocompartment encapsulin. Our engineered virus-like particle carries a dual functional artificial metalloenzyme (ArM) as non-native guest protein. This ArM, created from a fusion protein of HaloTag and monomeric rhizavidin, serves as catalyst for a fully bioorthogonal, linear, two-step reaction cascade. A ruthenium-catalyzed alloc deprotection is followed by a gold-catalyzed, ring-closing hydroamination reaction leading to indoles and phenanthridines with up to 67 % overall yield in aqueous solutions.

Supplementary materials

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Title
Sequential, all-bioorthogonal reaction cascade catalyzed by a dual functional artificial metalloenzyme inside encapsulin
Description
The supplementary material contains additional analytical data as well as synthetic procedures.
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