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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.

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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, Accepted Manuscript
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, C. L. Mackay, K. Waldron, J. Marles-Wright and D. Clarke, Chem. Commun., 2020, Accepted Manuscript , DOI: 10.1039/C9CC08130E

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