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Macromolecular organization of ATP synthase and complex I in whole mitochondria
by
Daum, Bertram
, Davies, Karen M
, Strauss, Mike
, Rycovska, Adriana
, Zickermann, Volker
, Kief, Jan H
, Kühlbrandt, Werner
, Osiewacz, Heinz D
in
Adenosine triphosphatase
/ adenosine triphosphate
/ Animals
/ ATP
/ ATP synthase
/ Biological Sciences
/ Cattle
/ Cristae
/ Dimers
/ Electron transport
/ Electron transport chain
/ Electron Transport Complex I - metabolism
/ Electron Transport Complex I - ultrastructure
/ Electrons
/ Fungi
/ Fungi - enzymology
/ H-transporting ATP synthase
/ Heads
/ Heart
/ Macromolecular Substances - metabolism
/ Macromolecules
/ Membranes
/ Mitochondria
/ Mitochondria - enzymology
/ Mitochondria - ultrastructure
/ Mitochondrial membranes
/ Mitochondrial Membranes - enzymology
/ Mitochondrial Membranes - ultrastructure
/ Mitochondrial Proton-Translocating ATPases - metabolism
/ Mitochondrial Proton-Translocating ATPases - ultrastructure
/ Monomers
/ P branes
/ Podospora
/ potatoes
/ Protein Multimerization
/ proton pump
/ Proton pumps
/ Protons
/ Saccharomyces cerevisiae
/ Solanum tuberosum
/ Solanum tuberosum - enzymology
/ Tomography
/ Ungulates
/ Yarrowia
/ Yeast
2011
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Macromolecular organization of ATP synthase and complex I in whole mitochondria
by
Daum, Bertram
, Davies, Karen M
, Strauss, Mike
, Rycovska, Adriana
, Zickermann, Volker
, Kief, Jan H
, Kühlbrandt, Werner
, Osiewacz, Heinz D
in
Adenosine triphosphatase
/ adenosine triphosphate
/ Animals
/ ATP
/ ATP synthase
/ Biological Sciences
/ Cattle
/ Cristae
/ Dimers
/ Electron transport
/ Electron transport chain
/ Electron Transport Complex I - metabolism
/ Electron Transport Complex I - ultrastructure
/ Electrons
/ Fungi
/ Fungi - enzymology
/ H-transporting ATP synthase
/ Heads
/ Heart
/ Macromolecular Substances - metabolism
/ Macromolecules
/ Membranes
/ Mitochondria
/ Mitochondria - enzymology
/ Mitochondria - ultrastructure
/ Mitochondrial membranes
/ Mitochondrial Membranes - enzymology
/ Mitochondrial Membranes - ultrastructure
/ Mitochondrial Proton-Translocating ATPases - metabolism
/ Mitochondrial Proton-Translocating ATPases - ultrastructure
/ Monomers
/ P branes
/ Podospora
/ potatoes
/ Protein Multimerization
/ proton pump
/ Proton pumps
/ Protons
/ Saccharomyces cerevisiae
/ Solanum tuberosum
/ Solanum tuberosum - enzymology
/ Tomography
/ Ungulates
/ Yarrowia
/ Yeast
2011
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Macromolecular organization of ATP synthase and complex I in whole mitochondria
by
Daum, Bertram
, Davies, Karen M
, Strauss, Mike
, Rycovska, Adriana
, Zickermann, Volker
, Kief, Jan H
, Kühlbrandt, Werner
, Osiewacz, Heinz D
in
Adenosine triphosphatase
/ adenosine triphosphate
/ Animals
/ ATP
/ ATP synthase
/ Biological Sciences
/ Cattle
/ Cristae
/ Dimers
/ Electron transport
/ Electron transport chain
/ Electron Transport Complex I - metabolism
/ Electron Transport Complex I - ultrastructure
/ Electrons
/ Fungi
/ Fungi - enzymology
/ H-transporting ATP synthase
/ Heads
/ Heart
/ Macromolecular Substances - metabolism
/ Macromolecules
/ Membranes
/ Mitochondria
/ Mitochondria - enzymology
/ Mitochondria - ultrastructure
/ Mitochondrial membranes
/ Mitochondrial Membranes - enzymology
/ Mitochondrial Membranes - ultrastructure
/ Mitochondrial Proton-Translocating ATPases - metabolism
/ Mitochondrial Proton-Translocating ATPases - ultrastructure
/ Monomers
/ P branes
/ Podospora
/ potatoes
/ Protein Multimerization
/ proton pump
/ Proton pumps
/ Protons
/ Saccharomyces cerevisiae
/ Solanum tuberosum
/ Solanum tuberosum - enzymology
/ Tomography
/ Ungulates
/ Yarrowia
/ Yeast
2011
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Macromolecular organization of ATP synthase and complex I in whole mitochondria
Journal Article
Macromolecular organization of ATP synthase and complex I in whole mitochondria
2011
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Overview
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.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Animals
/ ATP
/ Cattle
/ Cristae
/ Dimers
/ Electron Transport Complex I - metabolism
/ Electron Transport Complex I - ultrastructure
/ Fungi
/ Heads
/ Heart
/ Macromolecular Substances - metabolism
/ Mitochondria - ultrastructure
/ Mitochondrial Membranes - enzymology
/ Mitochondrial Membranes - ultrastructure
/ Mitochondrial Proton-Translocating ATPases - metabolism
/ Mitochondrial Proton-Translocating ATPases - ultrastructure
/ Monomers
/ P branes
/ potatoes
/ Protons
/ Solanum tuberosum - enzymology
/ Yarrowia
/ Yeast
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