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

Jennifer Ross, Thomas Lambert, Cecilia Piergentili, Didi He, Kevin J. Waldron, C. Logan Mackay, Jon Marles‐Wright, David J. Clarke

2020Chemical Communications20 citationsDOIOpen Access PDF

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.

Topics & Concepts

Mass spectrometryChemistryFerritinCeruloplasminHydrogen–deuterium exchangeBiochemistryChromatographyIron Metabolism and DisordersRNA and protein synthesis mechanismsTrace Elements in Health
Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface | Litcius