DOI: 10.1016/s0959-440x(00)00147-0. The rotary mechanism of ATP synthase

10.1016/s0959-440x(00)00147-0

Crossref journal-article

Elsevier BV

Current Opinion in Structural Biology (78)

Bibliography

Stock, D., Gibbons, C., Arechaga, I., Leslie, A. G., & Walker, J. E. (2000). The rotary mechanism of ATP synthase. Current Opinion in Structural Biology, 10(6), 672â679.

Authors 5

Daniela Stock (first)
Clyde Gibbons (additional)
Ignacio Arechaga (additional)
Andrew GW Leslie (additional)
John E Walker (additional)

References 63 Referenced 271

10.1146/annurev.biochem.66.1.717 / Annu Rev Biochem / The ATP synthase — a splendid molecular machine by Boyer (1997)
10.1002/(SICI)1521-3773(19980918)37:17<2308::AID-ANIE2308>3.0.CO;2-W / Angew Chem Int Ed Engl / ATP synthesis by rotary catalysis (Nobel Lecture) by Walker (1998)
10.1146/annurev.biophys.28.1.205 / Annu Rev Biophys Biomol Struct / Rotational coupling in the FoF1 ATP synthase by Nakamoto (1999)
10.1038/370621a0 / Nature / Structure at 2.8Å resolution of F1-ATPase from bovine heart mitochondria by Abrahams (1994)
10.1038/386299a0 / Nature / Direct observation of the rotation of F1-ATPase by Noji (1997)
10.1073/pnas.96.24.13697 / Proc Natl Acad Sci USA / Structural features of the gamma subunit of the Escherichia coli F1-ATPase revealed by a 4.4 Å resolution map obtained by X-ray crystallography by Hausrath (1999)
10.1016/S0969-2126(97)00272-4 / Structure / Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli by Uhlin (1997)
10.1074/jbc.274.40.28351 / J Biol Chem / The epsilon subunit of the F1Fo complex of Escherichia coli—cross-linking studies show the same structure in situ as when isolated by Schulenberg (1999)
10.1074/jbc.271.45.28341 / J Biol Chem / The stalk region of the Escherichia coli ATP synthase — tyrosine 205 of the gamma-subunit is in the interface between the F1 and Fo parts and can interact with both the epsilon and c oligomer by Watts (1996)
10.1074/jbc.271.6.3018 / J Biol Chem / Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase by Tang (1996)
10.1074/jbc.273.41.26645 / J Biol Chem / Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex by Wilkens (1998)
10.1074/jbc.270.16.9185 / J Biol Chem / Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences by Aggeler (1995)
10.1016/0005-2728(95)00040-P / Biochim Biophys Acta / Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit by Aggeler (1995)
10.1038/29908 / Nature / ATP synthase's second stalk comes into focus by Wilkens (1998)
10.1006/jmbi.1999.3435 / J Mol Biol / Direct visualisation of conformational changes in EFoF1 by electron microscopy by Bottcher (2000)
10.1006/jmbi.1998.1957 / J Mol Biol / Direct indication for the existence of a double stalk in CF0F1 by Bottcher (1998)
10.1006/jmbi.1999.2897 / J Mol Biol / Novel features in the structure of bovine ATP synthase by Karrasch (1999)
10.1074/jbc.274.43.31094 / J Biol Chem / The dimerization domain of the b subunit of the Escherichia coli F1Fo-ATPase by Revington (1999)
10.1074/jbc.274.22.15598 / J Biol Chem / Structure of the membrane domain of subunit b of the Escherichia coli FoF1 ATP synthase by Dmitriev (1999)
10.1016/S0022-2836(84)71591-9 / J Mol Biol / ATP synthase from bovine heart mitochondria — in vitro assembly of a stalk complex in the presence of F1-ATPase and in its absence by Collinson (1994)
10.1021/bi9916067 / Biochemistry / The second stalk of the yeast ATP synthase complex: identification of subunits showing cross-links with known positions of subunit 4 (subunit b) by Soubannier (1999)
10.1016/S0005-2728(00)00093-1 / Biochim Biophys Acta / Organisation of the yeast ATP synthase Fo: a study based on cysteine mutants, thiol modification and cross-linking reagents by Velours (2000)
10.1074/jbc.273.43.27873 / J Biol Chem / Deletions in the second stalk of F1Fo-ATP synthase in Escherichia coli by Sorgen (1998)
10.1074/jbc.274.51.36261 / J Biol Chem / Lengthening the second stalk of F1Fo-ATP synthase in Escherichia coli by Sorgen (1999)
10.1074/jbc.272.26.16652 / J Biol Chem / Cross-linking of the delta subunit to one of the three alpha subunits has no effect on functioning, as expected if delta is a part of the stator that links the F1 and Fo parts of the Escherichia coli ATP synthase by Ogilvie (1997)
10.1006/jmbi.1999.3381 / J Mol Biol / Localization of the delta subunit in the Escherichia coli F1Fo-ATP synthase by immune electron microscopy: the delta subunit binds on top of the F1 by Wilkens (2000)
10.1038/nsb0397-198 / Nat Struct Biol / Solution structure of the N-terminal domain of the delta subunit of the E. coli ATP synthase by Wilkens (1997)
10.1073/pnas.95.12.6607 / Proc Natl Acad Sci USA / Interacting helical faces of subunits a and c in the F1Fo-ATP synthase of Escherichia coli defined by disulfide cross-linking by Jiang (1998)
10.1016/S0005-2728(00)00094-3 / Biochim Biophys Acta / A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation by Vik (2000)
10.1074/jbc.273.26.16241 / J Biol Chem / Transmembrane topography of subunit a in the Escherichia coli F1Fo-ATP synthase by Valiyaveetil (1998)
10.1074/jbc.274.24.17353 / J Biol Chem / A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase by Wada (1999)
10.1021/bi980511m / Biochemistry / Solution structure of the transmembrane H+-transporting subunit c of the F1Fo-ATP synthase by Girvin (1998)
10.1021/bi00191a026 / Biochemistry / Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase by Collinson (1994)
10.1016/S0014-5793(97)00691-1 / FEBS Lett / Yeast mitochondrial F1Fo-ATPase: the novel subunit e is identical to Tim11 by Arnold (1997)
10.1074/jbc.274.1.36 / J Biol Chem / ATP synthase of yeast mitochondria. Isolation of subunit j and disruption of the ATP18 gene by Arnold (1999)
10.1126/science.286.5445.1700 / Science / Molecular architecture of the rotary motor in ATP synthase by Stock (1999)
10.1074/jbc.274.24.17011 / J Biol Chem / Defining the domain of binding of F1 subunit epsilon with the polar loop of Fo subunit c in the Escherichia coli ATP synthase by Hermolin (1999)
10.1074/jbc.272.24.15065 / J Biol Chem / Interactions between the F1 and Fo parts in the Escherichia coli ATP synthase. Associations involving the loop region of c subunits by Watts (1997)
10.1074/jbc.274.48.34233 / J Biol Chem / The gamma-epsilon-c subunit interface in the ATP synthase of Escherichia coli. Cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling by Schulenberg (1999)
10.1016/S0092-8674(00)81413-0 / Cell / Bacteriophage DNA packaging: RNA gears in a DNA transport machine by Hendrix (1998)
10.1016/S0969-2126(99)80039-2 / Structure / The three-dimensional structure of a DNA translocating machine at 10Å resolution by Valpuesta (1999)
10.1073/pnas.96.18.10134 / Proc Natl Acad Sci USA / Rotational symmetry of the c ring and a mechanism for the flagellar rotary motor by Thomas (1999)
10.1006/jsbi.1998.4039 / J Struct Biol / At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease by Beuron (1998)
10.1074/jbc.273.45.29701 / J Biol Chem / Genetic fusions of subunit c in the Fo sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis by Jones (1998)
10.1074/jbc.273.27.17178 / J Biol Chem / Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1Fo-ATP synthase by Jones (1998)
10.1038/35013148 / Nature / Proton-powered turbine of a plant motor by Seelert (2000)
10.1128/JB.180.12.3205-3208.1998 / J Bacteriol / Effects of carbon source on expression of Fo genes and on the stoichiometry of the c subunit in the F1Fo ATPase of Escherichia coli by Schemidt (1998)
10.1016/S0014-5793(99)00386-5 / FEBS Lett / Transient accumulation of elastic energy in proton translocating ATP synthase by Cherepanov (1999)
10.1016/S0005-2728(00)00096-7 / Biochim Biophys Acta / Reverse engineering a protein: the mechanochemistry of ATP synthase by Oster (2000)
10.1016/S0014-5793(99)01602-6 / FEBS Lett / The gamma subunit in chloroplast F1-ATPase can rotate in a unidirectional and counter-clockwise manner by Hisabori (1999)
10.1074/jbc.273.31.19375 / J Biol Chem / Direct observation of the rotation of epsilon subunit in F1-ATPase by Kato-Yamada (1998)
10.1006/bbrc.1999.0885 / Biochem Biophys Res Comm / Rotation of Escherichia coli F1-ATPase by Noji (1999)
10.1073/pnas.96.14.7780 / Proc Natl Acad Sci USA / The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli by Omote (1999)
10.1016/S0092-8674(00)81456-7 / Cell / F1-ATPase is a highly efficient molecular motor that rotates with discrete 120o steps by Yasuda (1998)
10.1126/science.286.5445.1722 / Science / Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation by Sambongi (1999)
10.1016/S0014-5793(00)01436-8 / FEBS Lett / F-ATPase: specific observation of the rotating c subunit oligomer of EFoEF1 by Panke (2000)
10.1016/S0014-5793(00)01336-3 / FEBS Lett / Observations of rotation within the FoFl-ATP synthase: deciding between rotation of the Foc-subunit ring and artifact by Tsunoda (2000)
10.1016/S0968-0004(97)01129-8 / Trends Biol Sci / ATP synthase: an electrochemical transducer with rotary mechanics by Junge (1997)
10.1038/35185 / Nature / Energy transduction in ATP synthase by Elston (1998)
10.1073/pnas.96.9.4924 / Proc Natl Acad Sci USA / Energy transduction in the sodium F-ATPase of Propionigenium modestum by Dimroth (1999)
10.1038/46224 / Nature / Structural changes linked to proton translocation by subunit c of the ATP synthase by Rastogi (1999)
10.1016/S0969-2126(00)00145-3 / Structure / Structure of bovine F1-ATPase inhibited by Mg2+ADP and aluminium fluoride by Braig (2000)
10.1038/80981 / Nat Struct Biol / The structure of the central stalk at 2.4Å resolution by Gibbons (2000)

Dates

Type	When
Created	23 years, 1 month ago (July 25, 2002, 12:59 p.m.)
Deposited	5 years, 7 months ago (Jan. 16, 2020, 11:36 p.m.)
Indexed	1 month, 2 weeks ago (July 7, 2025, 9:06 a.m.)
Issued	24 years, 8 months ago (Dec. 1, 2000)
Published	24 years, 8 months ago (Dec. 1, 2000)
Published Print	24 years, 8 months ago (Dec. 1, 2000)

Funders 0

None

BibTeX

@article{Stock_2000, title={The rotary mechanism of ATP synthase}, volume={10}, ISSN={0959-440X}, url={http://dx.doi.org/10.1016/s0959-440x(00)00147-0}, DOI={10.1016/s0959-440x(00)00147-0}, number={6}, journal={Current Opinion in Structural Biology}, publisher={Elsevier BV}, author={Stock, Daniela and Gibbons, Clyde and Arechaga, Ignacio and Leslie, Andrew GW and Walker, John E}, year={2000}, month=dec, pages={672–679} }

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      "author": "Wilkens",
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      "volume": "95",
      "author": "Jiang",
      "year": "1998",
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      "volume": "1458",
      "author": "Vik",
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      "author": "Valiyaveetil",
      "year": "1998",
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      "volume": "274",
      "author": "Wada",
      "year": "1999",
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      "first-page": "8817",
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      "volume": "37",
      "author": "Girvin",
      "year": "1998",
      "journal-title": "Biochemistry"
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      "DOI": "10.1021/bi00191a026",
      "article-title": "Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase",
      "volume": "33",
      "author": "Collinson",
      "year": "1994",
      "journal-title": "Biochemistry"
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      "volume": "411",
      "author": "Arnold",
      "year": "1997",
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      "volume": "274",
      "author": "Arnold",
      "year": "1999",
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      "author": "Stock",
      "year": "1999",
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      "volume": "274",
      "author": "Hermolin",
      "year": "1999",
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      "volume": "272",
      "author": "Watts",
      "year": "1997",
      "journal-title": "J Biol Chem"
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      "first-page": "34233",
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      "volume": "274",
      "author": "Schulenberg",
      "year": "1999",
      "journal-title": "J Biol Chem"
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      "first-page": "147",
      "DOI": "10.1016/S0092-8674(00)81413-0",
      "article-title": "Bacteriophage DNA packaging: RNA gears in a DNA transport machine",
      "volume": "94",
      "author": "Hendrix",
      "year": "1998",
      "journal-title": "Cell"
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      "first-page": "289",
      "DOI": "10.1016/S0969-2126(99)80039-2",
      "article-title": "The three-dimensional structure of a DNA translocating machine at 10\u00c5 resolution",
      "volume": "7",
      "author": "Valpuesta",
      "year": "1999",
      "journal-title": "Structure"
    },
    {
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      "first-page": "10134",
      "DOI": "10.1073/pnas.96.18.10134",
      "article-title": "Rotational symmetry of the c ring and a mechanism for the flagellar rotary motor",
      "volume": "96",
      "author": "Thomas",
      "year": "1999",
      "journal-title": "Proc Natl Acad Sci USA"
    },
    {
      "key": "10.1016/S0959-440X(00)00147-0_BIB43",
      "doi-asserted-by": "crossref",
      "first-page": "248",
      "DOI": "10.1006/jsbi.1998.4039",
      "article-title": "At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease",
      "volume": "123",
      "author": "Beuron",
      "year": "1998",
      "journal-title": "J Struct Biol"
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    {
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      "first-page": "29701",
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      "volume": "273",
      "author": "Jones",
      "year": "1998",
      "journal-title": "J Biol Chem"
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      "volume": "273",
      "author": "Jones",
      "year": "1998",
      "journal-title": "J Biol Chem"
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      "first-page": "418",
      "DOI": "10.1038/35013148",
      "article-title": "Proton-powered turbine of a plant motor",
      "volume": "405",
      "author": "Seelert",
      "year": "2000",
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      "first-page": "3205",
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      "volume": "180",
      "author": "Schemidt",
      "year": "1998",
      "journal-title": "J Bacteriol"
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      "first-page": "1",
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      "article-title": "Transient accumulation of elastic energy in proton translocating ATP synthase",
      "volume": "449",
      "author": "Cherepanov",
      "year": "1999",
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      "volume": "1458",
      "author": "Oster",
      "year": "2000",
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      "volume": "463",
      "author": "Hisabori",
      "year": "1999",
      "journal-title": "FEBS Lett"
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      "first-page": "19375",
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      "volume": "273",
      "author": "Kato-Yamada",
      "year": "1998",
      "journal-title": "J Biol Chem"
    },
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      "first-page": "597",
      "DOI": "10.1006/bbrc.1999.0885",
      "article-title": "Rotation of Escherichia coli F1-ATPase",
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      "author": "Noji",
      "year": "1999",
      "journal-title": "Biochem Biophys Res Comm"
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    {
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      "first-page": "7780",
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      "article-title": "The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli",
      "volume": "96",
      "author": "Omote",
      "year": "1999",
      "journal-title": "Proc Natl Acad Sci USA"
    },
    {
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      "first-page": "1117",
      "DOI": "10.1016/S0092-8674(00)81456-7",
      "article-title": "F1-ATPase is a highly efficient molecular motor that rotates with discrete 120o steps",
      "volume": "93",
      "author": "Yasuda",
      "year": "1998",
      "journal-title": "Cell"
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      "volume": "286",
      "author": "Sambongi",
      "year": "1999",
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      "article-title": "F-ATPase: specific observation of the rotating c subunit oligomer of EFoEF1",
      "volume": "472",
      "author": "Panke",
      "year": "2000",
      "journal-title": "FEBS Lett"
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      "DOI": "10.1016/S0014-5793(00)01336-3",
      "article-title": "Observations of rotation within the FoFl-ATP synthase: deciding between rotation of the Foc-subunit ring and artifact",
      "volume": "470",
      "author": "Tsunoda",
      "year": "2000",
      "journal-title": "FEBS Lett"
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      "first-page": "420",
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      "article-title": "ATP synthase: an electrochemical transducer with rotary mechanics",
      "volume": "22",
      "author": "Junge",
      "year": "1997",
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      "author": "Elston",
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      "article-title": "Energy transduction in the sodium F-ATPase of Propionigenium modestum",
      "volume": "96",
      "author": "Dimroth",
      "year": "1999",
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      "article-title": "Structural changes linked to proton translocation by subunit c of the ATP synthase",
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      "author": "Rastogi",
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      "DOI": "10.1016/S0969-2126(00)00145-3",
      "article-title": "Structure of bovine F1-ATPase inhibited by Mg2+ADP and aluminium fluoride",
      "volume": "8",
      "author": "Braig",
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      "author": "Gibbons",
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