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  Macromolecular organization of ATP synthase and complex I in whole mitochondria

Davies, K. M., Strauss, M., Daum, B., Kief, J. H., Osiewacz, H. D., Rycovska, A., et al. (2011). Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proceedings of the National Academy of Sciences of the United States of America, 108(34), 14121-14126. doi:10.1073/pnas.1103621108.

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 Creators:
Davies, Karen M.1, Author           
Strauss, Mike1, Author           
Daum, Bertram1, Author           
Kief, Jan H.2, 3, Author
Osiewacz, Heinz D.4, 5, Author
Rycovska, Adriana6, Author           
Zickermann, Volker7, Author
Kühlbrandt, Werner1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Mitochondrial Biology, Medical School, Goethe University Frankfurt, Frankfurt am Main, 60590 Frankfurt am Main, Germany, ou_persistent22              
3Mitochondrial Biology, Frankfurt Institute for Molecular Life Sciences, 60438 Frankfurt am Main, Germany, ou_persistent22              
4Molecular Developmental Biology, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
5Deutsche Forschungsgemeinschaft Cluster of Excellence Frankfurt “Macromolecular Complexes”, 60438 Frankfurt, Germany, ou_persistent22              
6Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
7Medical Faculty, Molecular Bioenergetics, Goethe University Frankfurt, 60590 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: cryoelectron tomography; subtomogram averaging; membrane curvature; membrane potential; mitochondrial ultrastructure
 Abstract: We used electron cryotomography to study the molecular arrangement of large respiratory chain complexes in mitochondria from bovine heart, potato, and three types of fungi. Long rows of ATP synthase dimers were observed in intact mitochondria and cristae membrane fragments of all species that were examined. The dimer rows were found exclusively on tightly curved cristae edges. The distance between dimers along the rows varied, but within the dimer the distance between F1 heads was constant. The angle between monomers in the dimer was 70° or above. Complex I appeared as L-shaped densities in tomograms of reconstituted proteoliposomes. Similar densities were observed in flat membrane regions of mitochondrial membranes from all species except Saccharomyces cerevisiae and identified as complex I by quantum-dot labeling. The arrangement of respiratory chain proton pumps on flat cristae membranes and ATP synthase dimer rows along cristae edges was conserved in all species investigated. We propose that the supramolecular organization of respiratory chain complexes as proton sources and ATP synthase rows as proton sinks in the mitochondrial cristae ensures optimal conditions for efficient ATP synthesis.

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Language(s): eng - English
 Dates: 2001-03-072011-07-012011-08-232011-08-23
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1103621108
PMID: 21836051
PMC: PMC3161574
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 108 (34) Sequence Number: - Start / End Page: 14121 - 14126 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230