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Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin

The iron redox cycle in ferritins is not completely understood. Bacterioferritins are distinct from other ferritins in that they contain haem groups. It is acknowledged that the two iron motifs in bacterioferritins, the di‐nuclear ferroxidase centre and the haem B group, play key roles in two opposi...

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Autores principales: Pullin, Jacob, Bradley, Justin M., Moore, Geoffrey R., Le Brun, Nick E., Wilson, Michael T., Svistunenko, Dimitri A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8048850/
https://www.ncbi.nlm.nih.gov/pubmed/33460502
http://dx.doi.org/10.1002/anie.202015965
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author Pullin, Jacob
Bradley, Justin M.
Moore, Geoffrey R.
Le Brun, Nick E.
Wilson, Michael T.
Svistunenko, Dimitri A.
author_facet Pullin, Jacob
Bradley, Justin M.
Moore, Geoffrey R.
Le Brun, Nick E.
Wilson, Michael T.
Svistunenko, Dimitri A.
author_sort Pullin, Jacob
collection PubMed
description The iron redox cycle in ferritins is not completely understood. Bacterioferritins are distinct from other ferritins in that they contain haem groups. It is acknowledged that the two iron motifs in bacterioferritins, the di‐nuclear ferroxidase centre and the haem B group, play key roles in two opposing processes, iron sequestration and iron mobilisation, respectively, and the two redox processes are independent. Herein, we show that in Escherichia coli bacterioferritin, there is an electron transfer pathway from the haem to the ferroxidase centre suggesting a new role(s) haem might play in bacterioferritins.
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spelling pubmed-80488502021-04-20 Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin Pullin, Jacob Bradley, Justin M. Moore, Geoffrey R. Le Brun, Nick E. Wilson, Michael T. Svistunenko, Dimitri A. Angew Chem Int Ed Engl Communications The iron redox cycle in ferritins is not completely understood. Bacterioferritins are distinct from other ferritins in that they contain haem groups. It is acknowledged that the two iron motifs in bacterioferritins, the di‐nuclear ferroxidase centre and the haem B group, play key roles in two opposing processes, iron sequestration and iron mobilisation, respectively, and the two redox processes are independent. Herein, we show that in Escherichia coli bacterioferritin, there is an electron transfer pathway from the haem to the ferroxidase centre suggesting a new role(s) haem might play in bacterioferritins. John Wiley and Sons Inc. 2021-03-01 2021-04-06 /pmc/articles/PMC8048850/ /pubmed/33460502 http://dx.doi.org/10.1002/anie.202015965 Text en © 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Pullin, Jacob
Bradley, Justin M.
Moore, Geoffrey R.
Le Brun, Nick E.
Wilson, Michael T.
Svistunenko, Dimitri A.
Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin
title Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin
title_full Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin
title_fullStr Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin
title_full_unstemmed Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin
title_short Electron Transfer from Haem to the Di‐Iron Ferroxidase Centre in Bacterioferritin
title_sort electron transfer from haem to the di‐iron ferroxidase centre in bacterioferritin
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8048850/
https://www.ncbi.nlm.nih.gov/pubmed/33460502
http://dx.doi.org/10.1002/anie.202015965
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