DOI: 10.1074/jbc.m113.527879. Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm

Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm

10.1074/jbc.m113.527879

Crossref journal-article

Elsevier BV

Journal of Biological Chemistry (78)

Bibliography

Steed, P. R., & Fillingame, R. H. (2014). Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm. Journal of Biological Chemistry, 289(4), 2127â2138.

Authors 2

P. Ryan Steed (first)
Robert H. Fillingame (additional)

References 65 Referenced 12

10.1038/35089509 / Nat. Rev. Mol. Cell Biol / ATP synthase—a marvellous rotary engine of the cell by Yoshida (2001)
10.1016/j.abb.2008.05.004 / Arch. Biochem. Biophys / The rotary mechanism of the ATP synthase by Nakamoto (2008)
10.1146/annurev.biochem.78.081307.104803 / Annu. Rev. Biochem / Essentials for ATP synthesis by F1F0 ATP synthases by von Ballmoos (2009)
10.1016/S0021-9258(19)68140-8 / J. Biol. Chem / Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli by Foster (1982)
10.1073/pnas.081424898 / Proc. Natl. Acad. Sci. U.S.A / The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10 by Jiang (2001)
10.1073/pnas.0403545101 / Proc. Natl. Acad. Sci. U.S.A / Thermophilic ATP synthase has a decamer c-ring: indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling by Mitome (2004)
10.1126/science.1111199 / Science / Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus by Meier (2005)
10.1038/sj.embor.7400517 / EMBO Rep / The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory by Pogoryelov (2005)
10.1073/pnas.1011099107 / Proc. Natl. Acad. Sci. U.S.A / Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria by Watt (2010)
10.1126/science.286.5445.1700 / Science / Molecular architecture of the rotary motor in ATP synthase by Stock (1999)
10.1096/fasebj.3.10.2526771 / FASEB J / A perspective of the binding change mechanism for ATP synthesis by Boyer (1989)
10.1038/370621a0 / Nature / Structure at 2.8 Å 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)
10.1016/S0014-5793(03)00394-6 / FEBS Lett / ATP synthesis driven by proton transport in F1F0-ATP synthase by Weber (2003)
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 F1F0 ATP synthase by Jones (1998)
10.1073/pnas.96.14.7785 / Proc. Natl. Acad. Sci. U.S.A / Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme by Dmitriev (1999)
10.1074/jbc.M109.006916 / J. Biol. Chem / Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase by Vollmar (2009)
10.1016/j.bbabio.2010.04.014 / Biochim. Biophys. Acta / Structural and energetic basis for H+ versus Na+ binding selectivity in ATP synthase Fo rotors by Krah (2010)
10.1038/nsmb.1678 / Nat. Struct. Mol. Biol / High-resolution structure of the rotor ring of a proton-dependent ATP synthase by Pogoryelov (2009)
10.1371/journal.pbio.1000443 / PLoS Biol / A new type of proton coordination in an F1F0-ATP synthase rotor ring by Preiss (2010)
10.1016/S0021-9258(18)89143-8 / J. Biol. Chem / H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and F0 but not F0-mediated H+ translocation by Mosher (1985)
10.1016/S0021-9258(17)31258-9 / J. Biol. Chem / Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0 by Miller (1989)
10.1016/S0021-9258(18)83500-1 / J. Biol. Chem / Conserved polar loop region of Escherichia coli subunit c of the F1F0 H+-ATPase. Glutamine 42 is not absolutely essential, but substitutions alter binding and coupling of F1 to F0 by Fraga (1989)
10.1016/0005-2728(93)90041-D / Biochim. Biophys. Acta / The role of arginine in the conserved polar loop of the c-subunit of the Escherichia coli H+-ATPase by Hatch (1993)
10.1016/S0021-9258(17)37319-2 / J. Biol. Chem / Arginine 41 of subunit c of the Escherichia coli H+-ATP synthase is essential in binding and coupling of F1 to F0 by Fraga (1994)
10.1016/S0021-9258(17)34049-8 / J. Biol. Chem / Suppressor mutations in F1 subunit ϵ recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase by Zhang (1994)
10.1074/jbc.270.41.24609 / J. Biol. Chem / Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase by Zhang (1995)
10.1016/0014-5793(95)00658-V / FEBS Lett / The γ subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part by Watts (1995)
10.1074/jbc.274.24.17011 / J. Biol. Chem / Defining the domain of binding of F1 subunit ϵ with the polar loop of F0 subunit c in the Escherichia coli ATP synthase by Hermolin (1999)
10.1111/j.1742-4658.2008.06623.x / FEBS J / Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus by Pogoryelov (2008)
10.1074/jbc.273.26.16241 / J. Biol. Chem / Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase by Valiyaveetil (1998)
10.1074/jbc.273.26.16235 / J. Biol. Chem / Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues by Long (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)
10.1074/jbc.M607453200 / J. Biol. Chem / Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle by Schwem (2006)
10.1073/pnas.95.12.6607 / Proc. Natl. Acad. Sci. U.S.A / Interacting helical faces of subunits a and c in the F1F0 ATP synthase of Eschericia coli defined by disulfide cross-linking by Jiang (1998)
10.1074/jbc.M803848200 / J. Biol. Chem / Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase by Moore (2008)
10.1016/S0014-5793(03)01101-3 / FEBS Lett / Mechanics of coupling proton movements to c-ring rotation in ATP synthase by Fillingame (2003)
10.1016/S0076-6879(98)93011-7 / Methods Enzymol / Substituted-cysteine accessibility method by Karlin (1998)
10.1073/pnas.0609968104 / Proc. Natl. Acad. Sci. U.S.A / Site-directed alkylation and the alternating access model for LacY by Kaback (2007)
10.1126/science.7716526 / Science / Silver as a probe of pore-forming residues in a potassium channel by Lü (1995)
10.1074/jbc.M210199200 / J. Biol. Chem / Aqueous access channels in subunit a of rotary ATP synthase by Angevine (2003)
10.1073/pnas.2234364100 / Proc. Natl. Acad. Sci. U.S.A / Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane by Angevine (2003)
10.1074/jbc.M610848200 / J. Biol. Chem / Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5 by Angevine (2007)
10.1074/jbc.M110.175844 / J. Biol. Chem / Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane by Dong (2010)
10.1074/jbc.M800900200 / J. Biol. Chem / The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism by Moore (2008)
10.1074/jbc.M800901200 / J. Biol. Chem / Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase by Steed (2008)
10.1074/jbc.M109.002501 / J. Biol. Chem / Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase by Steed (2009)
{'key': '10.1074/jbc.M113.527879_bib48', 'first-page': '203', 'article-title': 'Site-directed mutagenesis in vitro by megaprimer PCR', 'volume': '57', 'author': 'Barik', 'year': '1996', 'journal-title': 'Methods Mol. Biol'} / Methods Mol. Biol / Site-directed mutagenesis in vitro by megaprimer PCR by Barik (1996)
10.1074/jbc.275.15.11355 / J. Biol. Chem / Mutations in single hairpin units of genetically fused subunit c provide support for a rotary catalytic mechanism in F0F1 ATP synthase by Jones (2000)
10.1016/j.bbabio.2004.09.012 / Biochim. Biophys. Acta / Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1F0 ATP synthase by Ishmukhametov (2005)
10.1128/jb.160.3.1055-1060.1984 / J. Bacteriol / In vivo evidence for the role of the ϵ subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli by Klionsky (1984)
10.1016/j.bbabio.2008.06.008 / Biochim. Biophys. Acta / Δψ and ΔpH are equivalent driving forces for proton transport through isolated F0 complexes of ATP synthases by Wiedenmann (2008)
10.1016/S0021-9258(17)32992-7 / J. Biol. Chem / Purification of the carbodiimide-reactive protein component of the ATP energy-transducing system of Escherichia coli by Fillingame (1976)
10.1016/0076-6879(79)56050-9 / Methods Enzymol / A centrifuged-column procedure for the measurement of ligand binding by beef heart F1 by Penefsky (1979)
10.1016/j.bbabio.2007.05.007 / Biochim. Biophys. Acta / Essential arginine in subunit a and aspartate in subunit c of FoF1 ATP synthase: effect of repositioning within helix 4 of subunit a and helix 2 of subunit c by Langemeyer (2007)
10.1016/0005-2728(95)00040-P / Biochim. Biophys. Acta / Arrangement of the ϵ subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit by Aggeler (1995)
10.1021/bi901314c / Biochemistry / Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore by Alexander (2009)
10.1016/0076-6879(79)55058-7 / Methods Enzymol / Ionophores by Reed (1979)
10.1110/ps.072776307 / Protein Sci / The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c by Dmitriev (2007)
{'key': '10.1074/jbc.M113.527879_bib60', 'first-page': '9', 'article-title': 'Structural chemistry and geochemistry of silver-sulfur compounds: critical review', 'volume': '18', 'author': 'Bell', 'year': '1999', 'journal-title': 'Environ. Toxicol. Chem'} / Environ. Toxicol. Chem / Structural chemistry and geochemistry of silver-sulfur compounds: critical review by Bell (1999)
10.1074/jbc.M706904200 / J. Biol. Chem / Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking by Vincent (2007)
10.1074/jbc.M110.124529 / J. Biol. Chem / Crystal structure of the Mg·ADP-inhibited state of the yeast F1c10-ATP synthase by Dautant (2010)
10.1128/jb.173.8.2639-2643.1991 / J. Bacteriol / Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis by Fraga (1991)
{'key': '10.1074/jbc.M113.527879_bib64', 'series-title': 'Proton Transport at the Interface of Subunit c and the Rotor Ring of Escherichia coli ATP Synthase', 'author': 'Steed', 'year': '2010'} / Proton Transport at the Interface of Subunit c and the Rotor Ring of Escherichia coli ATP Synthase by Steed (2010)
10.1371/journal.pone.0043045 / PLoS One / Structure and flexibility of the C-ring in the electromotor of rotary F0F1-ATPase of pea chloroplasts by Saroussi (2012)

Dates

Type	When
Created	11 years, 8 months ago (Dec. 2, 2013, 9:11 p.m.)
Deposited	3 years, 7 months ago (Jan. 4, 2022, 12:49 a.m.)
Indexed	1 year, 4 months ago (April 1, 2024, 4:30 a.m.)
Issued	11 years, 7 months ago (Jan. 1, 2014)
Published	11 years, 7 months ago (Jan. 1, 2014)
Published Print	11 years, 7 months ago (Jan. 1, 2014)

Funders 0

None

BibTeX

@article{Steed_2014, title={Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm}, volume={289}, ISSN={0021-9258}, url={http://dx.doi.org/10.1074/jbc.m113.527879}, DOI={10.1074/jbc.m113.527879}, number={4}, journal={Journal of Biological Chemistry}, publisher={Elsevier BV}, author={Steed, P. Ryan and Fillingame, Robert H.}, year={2014}, month=jan, pages={2127–2138} }

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      "article-title": "Essentials for ATP synthesis by F1F0 ATP synthases",
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      "first-page": "4966",
      "DOI": "10.1073/pnas.081424898",
      "article-title": "The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10",
      "volume": "98",
      "author": "Jiang",
      "year": "2001",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
    },
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      "first-page": "12159",
      "DOI": "10.1073/pnas.0403545101",
      "article-title": "Thermophilic ATP synthase has a decamer c-ring: indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling",
      "volume": "101",
      "author": "Mitome",
      "year": "2004",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
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      "first-page": "659",
      "DOI": "10.1126/science.1111199",
      "article-title": "Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus",
      "volume": "308",
      "author": "Meier",
      "year": "2005",
      "journal-title": "Science"
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    {
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      "first-page": "1040",
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      "volume": "6",
      "author": "Pogoryelov",
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    {
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      "first-page": "16823",
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    {
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      "author": "Stock",
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      "first-page": "61",
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      "article-title": "ATP synthesis driven by proton transport in F1F0-ATP synthase",
      "volume": "545",
      "author": "Weber",
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      "article-title": "Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase",
      "volume": "273",
      "author": "Jones",
      "year": "1998",
      "journal-title": "J. Biol. Chem"
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    {
      "key": "10.1074/jbc.M113.527879_bib16",
      "doi-asserted-by": "crossref",
      "first-page": "7785",
      "DOI": "10.1073/pnas.96.14.7785",
      "article-title": "Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme",
      "volume": "96",
      "author": "Dmitriev",
      "year": "1999",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib17",
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      "first-page": "18228",
      "DOI": "10.1074/jbc.M109.006916",
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      "volume": "284",
      "author": "Vollmar",
      "year": "2009",
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      "DOI": "10.1016/j.bbabio.2010.04.014",
      "article-title": "Structural and energetic basis for H+ versus Na+ binding selectivity in ATP synthase Fo rotors",
      "volume": "1797",
      "author": "Krah",
      "year": "2010",
      "journal-title": "Biochim. Biophys. Acta"
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      "volume": "16",
      "author": "Pogoryelov",
      "year": "2009",
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    },
    {
      "key": "10.1074/jbc.M113.527879_bib20",
      "doi-asserted-by": "crossref",
      "first-page": "e1000443",
      "DOI": "10.1371/journal.pbio.1000443",
      "article-title": "A new type of proton coordination in an F1F0-ATP synthase rotor ring",
      "volume": "8",
      "author": "Preiss",
      "year": "2010",
      "journal-title": "PLoS Biol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib21",
      "doi-asserted-by": "crossref",
      "first-page": "4807",
      "DOI": "10.1016/S0021-9258(18)89143-8",
      "article-title": "H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and F0 but not F0-mediated H+ translocation",
      "volume": "260",
      "author": "Mosher",
      "year": "1985",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib22",
      "doi-asserted-by": "crossref",
      "first-page": "305",
      "DOI": "10.1016/S0021-9258(17)31258-9",
      "article-title": "Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0",
      "volume": "264",
      "author": "Miller",
      "year": "1989",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib23",
      "doi-asserted-by": "crossref",
      "first-page": "6797",
      "DOI": "10.1016/S0021-9258(18)83500-1",
      "article-title": "Conserved polar loop region of Escherichia coli subunit c of the F1F0 H+-ATPase. Glutamine 42 is not absolutely essential, but substitutions alter binding and coupling of F1 to F0",
      "volume": "264",
      "author": "Fraga",
      "year": "1989",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib24",
      "doi-asserted-by": "crossref",
      "first-page": "183",
      "DOI": "10.1016/0005-2728(93)90041-D",
      "article-title": "The role of arginine in the conserved polar loop of the c-subunit of the Escherichia coli H+-ATPase",
      "volume": "1141",
      "author": "Hatch",
      "year": "1993",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib25",
      "doi-asserted-by": "crossref",
      "first-page": "7532",
      "DOI": "10.1016/S0021-9258(17)37319-2",
      "article-title": "Arginine 41 of subunit c of the Escherichia coli H+-ATP synthase is essential in binding and coupling of F1 to F0",
      "volume": "269",
      "author": "Fraga",
      "year": "1994",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib26",
      "doi-asserted-by": "crossref",
      "first-page": "10221",
      "DOI": "10.1016/S0021-9258(17)34049-8",
      "article-title": "Suppressor mutations in F1 subunit \u03f5 recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase",
      "volume": "269",
      "author": "Zhang",
      "year": "1994",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib27",
      "doi-asserted-by": "crossref",
      "first-page": "24609",
      "DOI": "10.1074/jbc.270.41.24609",
      "article-title": "Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase",
      "volume": "270",
      "author": "Zhang",
      "year": "1995",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib28",
      "doi-asserted-by": "crossref",
      "first-page": "235",
      "DOI": "10.1016/0014-5793(95)00658-V",
      "article-title": "The \u03b3 subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part",
      "volume": "368",
      "author": "Watts",
      "year": "1995",
      "journal-title": "FEBS Lett"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib29",
      "doi-asserted-by": "crossref",
      "first-page": "17011",
      "DOI": "10.1074/jbc.274.24.17011",
      "article-title": "Defining the domain of binding of F1 subunit \u03f5 with the polar loop of F0 subunit c in the Escherichia coli ATP synthase",
      "volume": "274",
      "author": "Hermolin",
      "year": "1999",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib30",
      "doi-asserted-by": "crossref",
      "first-page": "4850",
      "DOI": "10.1111/j.1742-4658.2008.06623.x",
      "article-title": "Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus",
      "volume": "275",
      "author": "Pogoryelov",
      "year": "2008",
      "journal-title": "FEBS J"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib31",
      "doi-asserted-by": "crossref",
      "first-page": "16241",
      "DOI": "10.1074/jbc.273.26.16241",
      "article-title": "Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase",
      "volume": "273",
      "author": "Valiyaveetil",
      "year": "1998",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib32",
      "doi-asserted-by": "crossref",
      "first-page": "16235",
      "DOI": "10.1074/jbc.273.26.16235",
      "article-title": "Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues",
      "volume": "273",
      "author": "Long",
      "year": "1998",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib33",
      "doi-asserted-by": "crossref",
      "first-page": "17353",
      "DOI": "10.1074/jbc.274.24.17353",
      "article-title": "A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase",
      "volume": "274",
      "author": "Wada",
      "year": "1999",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib34",
      "doi-asserted-by": "crossref",
      "first-page": "37861",
      "DOI": "10.1074/jbc.M607453200",
      "article-title": "Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle",
      "volume": "281",
      "author": "Schwem",
      "year": "2006",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib35",
      "doi-asserted-by": "crossref",
      "first-page": "6607",
      "DOI": "10.1073/pnas.95.12.6607",
      "article-title": "Interacting helical faces of subunits a and c in the F1F0 ATP synthase of Eschericia coli defined by disulfide cross-linking",
      "volume": "95",
      "author": "Jiang",
      "year": "1998",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib36",
      "doi-asserted-by": "crossref",
      "first-page": "31726",
      "DOI": "10.1074/jbc.M803848200",
      "article-title": "Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase",
      "volume": "283",
      "author": "Moore",
      "year": "2008",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib37",
      "doi-asserted-by": "crossref",
      "first-page": "29",
      "DOI": "10.1016/S0014-5793(03)01101-3",
      "article-title": "Mechanics of coupling proton movements to c-ring rotation in ATP synthase",
      "volume": "555",
      "author": "Fillingame",
      "year": "2003",
      "journal-title": "FEBS Lett"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib38",
      "doi-asserted-by": "crossref",
      "first-page": "123",
      "DOI": "10.1016/S0076-6879(98)93011-7",
      "article-title": "Substituted-cysteine accessibility method",
      "volume": "293",
      "author": "Karlin",
      "year": "1998",
      "journal-title": "Methods Enzymol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib39",
      "doi-asserted-by": "crossref",
      "first-page": "491",
      "DOI": "10.1073/pnas.0609968104",
      "article-title": "Site-directed alkylation and the alternating access model for LacY",
      "volume": "104",
      "author": "Kaback",
      "year": "2007",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib40",
      "doi-asserted-by": "crossref",
      "first-page": "304",
      "DOI": "10.1126/science.7716526",
      "article-title": "Silver as a probe of pore-forming residues in a potassium channel",
      "volume": "268",
      "author": "L\u00fc",
      "year": "1995",
      "journal-title": "Science"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib41",
      "doi-asserted-by": "crossref",
      "first-page": "6066",
      "DOI": "10.1074/jbc.M210199200",
      "article-title": "Aqueous access channels in subunit a of rotary ATP synthase",
      "volume": "278",
      "author": "Angevine",
      "year": "2003",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib42",
      "doi-asserted-by": "crossref",
      "first-page": "13179",
      "DOI": "10.1073/pnas.2234364100",
      "article-title": "Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane",
      "volume": "100",
      "author": "Angevine",
      "year": "2003",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib43",
      "doi-asserted-by": "crossref",
      "first-page": "9001",
      "DOI": "10.1074/jbc.M610848200",
      "article-title": "Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5",
      "volume": "282",
      "author": "Angevine",
      "year": "2007",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib44",
      "doi-asserted-by": "crossref",
      "first-page": "39811",
      "DOI": "10.1074/jbc.M110.175844",
      "article-title": "Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane",
      "volume": "285",
      "author": "Dong",
      "year": "2010",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib45",
      "doi-asserted-by": "crossref",
      "first-page": "13044",
      "DOI": "10.1074/jbc.M800900200",
      "article-title": "The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism",
      "volume": "283",
      "author": "Moore",
      "year": "2008",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib46",
      "doi-asserted-by": "crossref",
      "first-page": "12365",
      "DOI": "10.1074/jbc.M800901200",
      "article-title": "Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase",
      "volume": "283",
      "author": "Steed",
      "year": "2008",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib47",
      "doi-asserted-by": "crossref",
      "first-page": "23243",
      "DOI": "10.1074/jbc.M109.002501",
      "article-title": "Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase",
      "volume": "284",
      "author": "Steed",
      "year": "2009",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib48",
      "first-page": "203",
      "article-title": "Site-directed mutagenesis in vitro by megaprimer PCR",
      "volume": "57",
      "author": "Barik",
      "year": "1996",
      "journal-title": "Methods Mol. Biol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib49",
      "doi-asserted-by": "crossref",
      "first-page": "11355",
      "DOI": "10.1074/jbc.275.15.11355",
      "article-title": "Mutations in single hairpin units of genetically fused subunit c provide support for a rotary catalytic mechanism in F0F1 ATP synthase",
      "volume": "275",
      "author": "Jones",
      "year": "2000",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib50",
      "doi-asserted-by": "crossref",
      "first-page": "110",
      "DOI": "10.1016/j.bbabio.2004.09.012",
      "article-title": "Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1F0 ATP synthase",
      "volume": "1706",
      "author": "Ishmukhametov",
      "year": "2005",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib51",
      "doi-asserted-by": "crossref",
      "first-page": "1055",
      "DOI": "10.1128/jb.160.3.1055-1060.1984",
      "article-title": "In vivo evidence for the role of the \u03f5 subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli",
      "volume": "160",
      "author": "Klionsky",
      "year": "1984",
      "journal-title": "J. Bacteriol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib52",
      "doi-asserted-by": "crossref",
      "first-page": "1301",
      "DOI": "10.1016/j.bbabio.2008.06.008",
      "article-title": "\u0394\u03c8 and \u0394pH are equivalent driving forces for proton transport through isolated F0 complexes of ATP synthases",
      "volume": "1777",
      "author": "Wiedenmann",
      "year": "2008",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib53",
      "doi-asserted-by": "crossref",
      "first-page": "6630",
      "DOI": "10.1016/S0021-9258(17)32992-7",
      "article-title": "Purification of the carbodiimide-reactive protein component of the ATP energy-transducing system of Escherichia coli",
      "volume": "251",
      "author": "Fillingame",
      "year": "1976",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib54",
      "doi-asserted-by": "crossref",
      "first-page": "527",
      "DOI": "10.1016/0076-6879(79)56050-9",
      "article-title": "A centrifuged-column procedure for the measurement of ligand binding by beef heart F1",
      "volume": "56",
      "author": "Penefsky",
      "year": "1979",
      "journal-title": "Methods Enzymol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib55",
      "doi-asserted-by": "crossref",
      "first-page": "998",
      "DOI": "10.1016/j.bbabio.2007.05.007",
      "article-title": "Essential arginine in subunit a and aspartate in subunit c of FoF1 ATP synthase: effect of repositioning within helix 4 of subunit a and helix 2 of subunit c",
      "volume": "1767",
      "author": "Langemeyer",
      "year": "2007",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib56",
      "doi-asserted-by": "crossref",
      "first-page": "62",
      "DOI": "10.1016/0005-2728(95)00040-P",
      "article-title": "Arrangement of the \u03f5 subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit",
      "volume": "1230",
      "author": "Aggeler",
      "year": "1995",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib57",
      "doi-asserted-by": "crossref",
      "first-page": "10078",
      "DOI": "10.1021/bi901314c",
      "article-title": "Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore",
      "volume": "48",
      "author": "Alexander",
      "year": "2009",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib58",
      "doi-asserted-by": "crossref",
      "first-page": "435",
      "DOI": "10.1016/0076-6879(79)55058-7",
      "article-title": "Ionophores",
      "volume": "55",
      "author": "Reed",
      "year": "1979",
      "journal-title": "Methods Enzymol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib59",
      "doi-asserted-by": "crossref",
      "first-page": "2118",
      "DOI": "10.1110/ps.072776307",
      "article-title": "The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c",
      "volume": "16",
      "author": "Dmitriev",
      "year": "2007",
      "journal-title": "Protein Sci"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib60",
      "first-page": "9",
      "article-title": "Structural chemistry and geochemistry of silver-sulfur compounds: critical review",
      "volume": "18",
      "author": "Bell",
      "year": "1999",
      "journal-title": "Environ. Toxicol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib61",
      "doi-asserted-by": "crossref",
      "first-page": "33788",
      "DOI": "10.1074/jbc.M706904200",
      "article-title": "Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking",
      "volume": "282",
      "author": "Vincent",
      "year": "2007",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib62",
      "doi-asserted-by": "crossref",
      "first-page": "29502",
      "DOI": "10.1074/jbc.M110.124529",
      "article-title": "Crystal structure of the Mg\u00b7ADP-inhibited state of the yeast F1c10-ATP synthase",
      "volume": "285",
      "author": "Dautant",
      "year": "2010",
      "journal-title": "J. Biol. Chem"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib63",
      "doi-asserted-by": "crossref",
      "first-page": "2639",
      "DOI": "10.1128/jb.173.8.2639-2643.1991",
      "article-title": "Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis",
      "volume": "173",
      "author": "Fraga",
      "year": "1991",
      "journal-title": "J. Bacteriol"
    },
    {
      "key": "10.1074/jbc.M113.527879_bib64",
      "series-title": "Proton Transport at the Interface of Subunit c and the Rotor Ring of Escherichia coli ATP Synthase",
      "author": "Steed",
      "year": "2010"
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    {
      "key": "10.1074/jbc.M113.527879_bib65",
      "doi-asserted-by": "crossref",
      "first-page": "e43045",
      "DOI": "10.1371/journal.pone.0043045",
      "article-title": "Structure and flexibility of the C-ring in the electromotor of rotary F0F1-ATPase of pea chloroplasts",
      "volume": "7",
      "author": "Saroussi",
      "year": "2012",
      "journal-title": "PLoS One"
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