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FEBS Letters, ISSN 0014-5793, 04/2000, Volume 472, Issue 1, pp. 34 - 38
The rotary motion in response to ATP hydrolysis of the ring of c subunits of the membrane portion, F(o), of ATP synthase, F(o)F , is still under contention. It... 
ATP synthase | EF(o)EF | Subunit c | Rotation | Single molecule
Journal Article
FEBS Letters, ISSN 0014-5793, 04/2000, Volume 472, Issue 1, pp. 34 - 38
The rotary motion in response to ATP hydrolysis of the ring of c subunits of the membrane portion, Fo, of ATP synthase, FoF1, is still under contention. It was... 
ATP synthase | Subunit c | Rotation | EFoEF1 | Single molecule | DIRECTED MUTAGENESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | rotation | F-1-ATPASE | CROSS-LINKING | ESCHERICHIA-COLI F1-ATPASE | EPSILON-SUBUNIT | CELL BIOLOGY | single molecule | SYNTHASE | BIOPHYSICS | subunit c | PURIFICATION | ELASTIC ENERGY | GAMMA-SUBUNIT | BETA-SUBUNIT
Journal Article
NATURE, ISSN 0028-0836, 05/2009, Volume 459, Issue 7245, pp. 364 - 370
Adenosine triphosphate (ATP), the universal fuel of the cell, is synthesized from adenosine diphosphate (ADP) and inorganic phosphate (Pi) by 'ATP synthase'... 
COUPLING PROTON MOVEMENTS | OXIDATIVE-PHOSPHORYLATION | NUCLEOTIDE DEPENDENCE | BOVINE HEART-MITOCHONDRIA | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | F-ATPASE | COLI ATP SYNTHASE | CATALYTIC SITES | C SUBUNIT OLIGOMER | B-SUBUNIT
Journal Article
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 07/2012, Volume 109, Issue 28, pp. 11139 - 11143
The molecular description of the mechanism of F-1-ATPase is based mainly on high-resolution structures of the enzyme from mitochondria, coupled with direct... 
ROTATION | catalytic mechanism | MECHANISM | YEAST F-1 ATPASE | MOLECULE | MULTIDISCIPLINARY SCIENCES | RESOLUTION | nucleotide release | CRYSTAL-STRUCTURES | magnesium release | C SUBUNIT OLIGOMER | ADP | FEATURES | SYNTHASE
Journal Article
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 12/2003, Volume 100, Issue 25, pp. 14731 - 14736
F-1, a water-soluble portion of FoF1-ATP synthase, is an ATIP hydrolysis-driven rotary motor. The central gamma-subunit rotates in the alpha(3)beta(3) cylinder... 
WILD-TYPE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | F-1-ATPASE | HEART MITOCHONDRIAL ATPASE | APPARENT NEGATIVE COOPERATIVITY | GLUTAMIC-ACID | GAMMA-SUBUNIT | BETA-SUBUNIT | THERMOPHILIC BACTERIUM | C-SUBUNIT OLIGOMER
Journal Article
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 07/2009, Volume 284, Issue 27, pp. 18228 - 18235
The structure of the membrane integral rotor ring of the proton translocating F1F0 ATP synthase from spinach chloroplasts was determined to 3.8 angstrom... 
NA+-ATPASE | ROTATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | F-ATPASE | BOVINE F-1-ATPASE | RESOLUTION | CROSS-LINKING | MODEL | AQUEOUS ACCESS | ROTARY MOTOR | C-SUBUNIT OLIGOMER
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 2010, Volume 1797, Issue 8, pp. 1343 - 1352
Two proton pumps, the F-ATPase (ATP synthase, F F ) and the V-ATPase (endomembrane proton pump), have different physiological functions, but are similar in... 
ATP synthase | Thermodynamic analysis | V-ATPase | Single molecule observation | F-ATPase | Subunit rotation | GLYCINE-RICH SEQUENCE | 3 CATALYTIC SITES | BOVINE HEART-MITOCHONDRIA | BIOCHEMISTRY & MOLECULAR BIOLOGY | CARBOXYL-TERMINAL REGION | ESCHERICHIA-COLI | VACUOLAR H+-ATPASE | BIOPHYSICS | COLI ATP SYNTHASE | GAMMA-SUBUNIT | BETA-SUBUNIT | C-SUBUNIT OLIGOMER
Journal Article
Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, 02/2002, Volume 1553, Issue 3, pp. 188 - 211
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 03/2002, Volume 27, Issue 3, pp. 154 - 160
The F F -type ATP synthase is a key enzyme in cellular energy interconversion. During ATP synthesis, this large protein complex uses a proton gradient and the... 
ALPHA-SUBUNITS | ROTATION | BOVINE HEART-MITOCHONDRIA | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | CONFORMATIONAL CHANGE | CATALYTIC SITES | BINDING | C-SUBUNIT OLIGOMER | ESCHERICHIA-COLI F1-ATPASE | EPSILON-SUBUNIT
Journal Article