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  The unusual homodimer of a heme‐copper terminal oxidase allows itself to utilize two electron donors

Zhu, G., Zeng, H., Zhang, S., Juli, J., Tai, L., Zhang, D., et al. (2021). The unusual homodimer of a heme‐copper terminal oxidase allows itself to utilize two electron donors. Angewandte Chemie, International Edition in English. doi:10.1002/anie.202016785.

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 Creators:
Zhu, Guoliang1, 2, Author
Zeng, Hui3, Author              
Zhang, Shuangbo1, 2, Author
Juli, Jana3, Author              
Tai, Linhua1, 2, Author
Zhang, Danyang1, 2, Author
Pang , Xiaoyun 1, Author
Zhang, Yan1, 2, Author
Lam, Sin Man4, 5, Author
Zhu, Yun1, 2, Author
Peng, Guohong1, 3, Author              
Michel, Hartmut3, Author              
Sun, Fei1, 2, 6, Author
Affiliations:
1National Key Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China, 15 Datun Road, Chaoyang District, Beijing, 100101, China, ou_persistent22              
2College of Life Sciences, University of Chinese Academy of Sciences, Beijing, 100049, China, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
4State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology Chinese Academy of Sciences, Beijing, 100101, China , No. 1 West Beichen Raod, Chaoyang District, Beijing, 100101, China , ou_persistent22              
5LipidAll Technologies Company Ltd, Changzhou 213022, Jiangsu Province, China, ou_persistent22              
6Center for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China, 15 Datun Road, Chaoyang District, Beijing, 100101, China, ou_persistent22              

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Free keywords: cytochrome c oxidase; protein structures; dimerization; enzyme catalysis; naphthoquinone
 Abstract: 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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Language(s): eng - English
 Dates: 2021-02-092020-12-182021-03-012021-03-042021
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.202016785
PMID: 33665933
 Degree: -

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Title: Angewandte Chemie, International Edition in English
  Abbreviation : Angew. Chem., Int. Ed. Engl.
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833