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Inside a Shell-Organometallic Catalysis Inside Encapsulin Nanoreactors.

Philipp Lohner¹, Mariia Zmyslia¹, Johann Thurn²

¹Department of Pharmaceutical Biology and Biotechnology, University of Freiburg, Stefan-Meier-Str. 19, 79104, Freiburg, Germany.

Angewandte Chemie (International Ed. in English)

|August 21, 2021

Summary

Researchers engineered protein nanocompartments called encapsulins for precise intracellular catalysis. These synthetic biological systems enable targeted chemical reactions within living cells, advancing synthetic biology applications.

Keywords:

MINFLUX encapsulins homogeneous catalysis self-assembly single-molecule FRET

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Area of Science:

Synthetic biology
Biochemistry
Nanotechnology

Background:

Cellular compartmentalization is essential for life.
Encapsulins are self-assembling protein nanocompartments from prokaryotes.
They offer a platform for designed intracellular reactions.

Purpose of the Study:

To analyze encapsulin structure and dynamics using single-molecule techniques.
To engineer encapsulins for hosting synthetic catalysts.
To demonstrate intracellular transition metal catalysis within engineered encapsulins.

Main Methods:

Single-molecule Förster resonance energy transfer (smFRET)
3D-MINFLUX super-resolution microscopy
Covalent attachment of ruthenium catalysts to host proteins
In vitro and in vivo catalysis assays

Main Results:

Single-molecule analysis of fluorescently labeled encapsulins.
Successful covalent attachment of a synthetic ruthenium catalyst.
Demonstration of in vitro catalysis using engineered encapsulins.
Evidence of transition metal catalysis within living cells using engineered encapsulins.

Conclusions:

Engineered encapsulins serve as effective hosts for intracellular catalysis.
This work enables precise spatial control of chemical reactions in living cells.
Encapsulins represent a promising tool for synthetic biology and nanotechnology.