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

doi:10.1039/C9CC08130E

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

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Journal	Chemical Communications
Early online date	13 Feb 2020
DOIs	https://doi.org/10.1039/C9CC08130E
Publication status	E-pub ahead of print - 13 Feb 2020

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10.1039/C9CC08130E

20200303_Clarke_c9cc08130eFinal published version, 2.29 MBLicence: Creative Commons: Attribution Non-Commercial (CC-BY-NC)

http://xlink.rsc.org/?DOI=C9CC08130E

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title = "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.",

author = "Jennifer Ross and Thomas Lambert and Cecilia Piergentili and Didi He and Waldron, {Kevin J.} and Mackay, {C. Logan} and Jon Marles-wright and Clarke, {David J.}",

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T1 - Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface

AU - Ross, Jennifer

AU - Lambert, Thomas

AU - Piergentili, Cecilia

AU - He, Didi

AU - Waldron, Kevin J.

AU - Mackay, C. Logan

AU - Marles-wright, Jon

AU - Clarke, David J.

PY - 2020/2/13

Y1 - 2020/2/13

N2 - 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.

AB - 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.

U2 - 10.1039/C9CC08130E

DO - 10.1039/C9CC08130E

M3 - Article

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

ER -

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

Abstract

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