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The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors

The heme‐copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B‐family cytochrome c oxidase from the hyperthermophilic bacterium Aquifex aeolicus was discovered previously to...

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Autores principales: Zhu, Guoliang, Zeng, Hui, Zhang, Shuangbo, Juli, Jana, Tai, Linhua, Zhang, Danyang, Pang, Xiaoyun, Zhang, Yan, Lam, Sin Man, Zhu, Yun, Peng, Guohong, Michel, Hartmut, Sun, Fei
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/PMC8251803/
https://www.ncbi.nlm.nih.gov/pubmed/33665933
http://dx.doi.org/10.1002/anie.202016785
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author Zhu, Guoliang
Zeng, Hui
Zhang, Shuangbo
Juli, Jana
Tai, Linhua
Zhang, Danyang
Pang, Xiaoyun
Zhang, Yan
Lam, Sin Man
Zhu, Yun
Peng, Guohong
Michel, Hartmut
Sun, Fei
author_facet Zhu, Guoliang
Zeng, Hui
Zhang, Shuangbo
Juli, Jana
Tai, Linhua
Zhang, Danyang
Pang, Xiaoyun
Zhang, Yan
Lam, Sin Man
Zhu, Yun
Peng, Guohong
Michel, Hartmut
Sun, Fei
author_sort Zhu, Guoliang
collection PubMed
description The heme‐copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B‐family cytochrome c oxidase from the hyperthermophilic bacterium Aquifex aeolicus was discovered previously to be able to use both cytochrome c and naphthoquinol as electron donors. Its molecular mechanism as well as the evolutionary significance are yet unknown. Here we solved its 3.4 Å resolution electron cryo‐microscopic structure and discovered a novel dimeric structure mediated by subunit I (CoxA2) that would be essential for naphthoquinol binding and oxidation. The unique structural features in both proton and oxygen pathways suggest an evolutionary adaptation of this oxidase to its hyperthermophilic environment. Our results add a new conceptual understanding of structural variation of cytochrome c oxidases in different species.
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spelling pubmed-82518032021-07-07 The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors Zhu, Guoliang Zeng, Hui Zhang, Shuangbo Juli, Jana Tai, Linhua Zhang, Danyang Pang, Xiaoyun Zhang, Yan Lam, Sin Man Zhu, Yun Peng, Guohong Michel, Hartmut Sun, Fei Angew Chem Int Ed Engl Research Articles The heme‐copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B‐family cytochrome c oxidase from the hyperthermophilic bacterium Aquifex aeolicus was discovered previously to be able to use both cytochrome c and naphthoquinol as electron donors. Its molecular mechanism as well as the evolutionary significance are yet unknown. Here we solved its 3.4 Å resolution electron cryo‐microscopic structure and discovered a novel dimeric structure mediated by subunit I (CoxA2) that would be essential for naphthoquinol binding and oxidation. The unique structural features in both proton and oxygen pathways suggest an evolutionary adaptation of this oxidase to its hyperthermophilic environment. Our results add a new conceptual understanding of structural variation of cytochrome c oxidases in different species. John Wiley and Sons Inc. 2021-05-06 2021-06-07 /pmc/articles/PMC8251803/ /pubmed/33665933 http://dx.doi.org/10.1002/anie.202016785 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 Research Articles
Zhu, Guoliang
Zeng, Hui
Zhang, Shuangbo
Juli, Jana
Tai, Linhua
Zhang, Danyang
Pang, Xiaoyun
Zhang, Yan
Lam, Sin Man
Zhu, Yun
Peng, Guohong
Michel, Hartmut
Sun, Fei
The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors
title The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors
title_full The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors
title_fullStr The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors
title_full_unstemmed The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors
title_short The Unusual Homodimer of a Heme‐Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors
title_sort unusual homodimer of a heme‐copper terminal oxidase allows itself to utilize two electron donors
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8251803/
https://www.ncbi.nlm.nih.gov/pubmed/33665933
http://dx.doi.org/10.1002/anie.202016785
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