Issue 23, 2020

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

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

Supplementary files

Article information

Article type
Communication
Submitted
16 Oct 2019
Accepted
13 Feb 2020
First published
13 Feb 2020
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2020,56, 3417-3420

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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