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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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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. |
format | Online Article Text |
id | pubmed-8048850 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
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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