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Issue 23, 2020
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Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface

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Abstract

Encapsulated ferritins (EncFtn) are a recently characterised member of the ferritin superfamily. EncFtn proteins are sequestered within encapsulin nanocompartments and form a unique biological iron storage system. Here, we use native mass spectrometry and hydrogen–deuterium exchange mass spectrometry to elucidate the metal-mediated assembly pathway of EncFtn.

Graphical abstract: Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface

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Article information


Submitted
16 Oct 2019
Accepted
13 Feb 2020
First published
13 Feb 2020

This article is Open Access

Chem. Commun., 2020,56, 3417-3420
Article type
Communication

Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface

J. Ross, T. Lambert, C. Piergentili, D. He, K. J. Waldron, C. L. Mackay, J. Marles-Wright and D. J. Clarke, Chem. Commun., 2020, 56, 3417
DOI: 10.1039/C9CC08130E

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