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  Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors

Gao, Y., Meyer, B., Sokolova, L., Zwicker, K., Karas, M., Brutschy, B., et al. (2012). Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors. Proceedings of the National Academy of Sciences of the United States of America, 109(9), 3275-3280. doi:10.1073/pnas.1121040109.

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 Creators:
Gao, Ye1, Author           
Meyer, Björn2, Author
Sokolova, Lucie3, Author
Zwicker, Klaus4, Author
Karas, Michael2, Author
Brutschy, Bernd3, Author
Peng, Guohong1, 5, Author           
Michel, Hartmut1, Author                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institute of Pharmaceutical Chemistry, Goethe University, 60438 Frankfurt, Germany, ou_persistent22              
3Institute of Physics and Theoretical Chemistry, Goethe University, 60438 Frankfurt, Germany, ou_persistent22              
4Molecular Bioenergetics, Medical School, Goethe University, 60590 Frankfurt, Germany, ou_persistent22              
5Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China, ou_persistent22              

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Free keywords: cytochrome c oxidase; quinol oxidase; cyanide inhibition; protein complex interaction
 Abstract: The cytochrome c oxidase Cox2 has been purified from native membranes of the hyperthermophilic eubacterium Aquifex aeolicus. It is a cytochrome ba3 oxidase belonging to the family B of the heme-copper containing terminal oxidases. It consists of three subunits, subunit I (CoxA2, 63.9 kDa), subunit II (CoxB2, 16.8 kDa), and an additional subunit IIa of 5.2 kDa. Surprisingly it is able to oxidize both reduced cytochrome c and ubiquinol in a cyanide sensitive manner. Cox2 is part of a respiratory chain supercomplex. This supercomplex contains the fully assembled cytochrome bc1 complex and Cox2. Although direct ubiquinol oxidation by Cox2 conserves less energy than ubiquinol oxidation by the cytochrome bc1 complex followed by cytochrome c oxidation by a cytochrome c oxidase, ubiquinol oxidation by Cox2 is of advantage when all ubiquinone would be completely reduced to ubiquinol, e.g., by the sulfide∶quinone oxidoreductase, because the cytochrome bc1 complex requires the presence of ubiquinone to function according to the Q-cycle mechanism. In the case that all ubiquinone has been reduced to ubiquinol its reoxidation by Cox2 will enable the cytochrome bc1 complex to resume working.

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Language(s): eng - English
 Dates: 2012-02-142012-02-28
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1121040109
PMID: 22334648
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 109 (9) Sequence Number: - Start / End Page: 3275 - 3280 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230