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Volumn 41, Issue 1, 2013, Pages 1-16

The ATP synthase: The understood, the uncertain and the unknown

Author keywords

Adenosine triphosphate (ATP); ATP synthase; Bacterium; Chloroplast; Energy cost; Mitochondrion; Protonmotive force; Rotor; Stator

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; HISTIDINE; MITOCHONDRIAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84873120174     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20110773     Document Type: Article
Times cited : (462)

References (119)
  • 2
    • 77955955395 scopus 로고    scopus 로고
    • A pore way to die: The role of mitochondria in reperfusion injury and cardioprotection
    • Halestrap, A. P. (2010) A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection. Biochem. Soc. Trans. 38, 841-860
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 841-860
    • Halestrap, A.P.1
  • 3
    • 81155124280 scopus 로고    scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation
    • Mitchell, P. (2011) Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biochim. Biophys. Acta 1807, 1507-1538
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1507-1538
    • Mitchell, P.1
  • 4
    • 33746819399 scopus 로고
    • David Keilin's respiratory chain concept and its chemiosmotic consequences
    • Frãnsmyr, T. and Forsé n, S., eds, World Scientific Publishing Co, Singapore
    • Mitchell, P. (1993) David Keilin's respiratory chain concept and its chemiosmotic consequences. In Nobel Lectures in Chemistry 1971-1980 (Frãnsmyr, T. and Forsé n, S., eds), pp. 295-330, World Scientific Publishing Co, Singapore
    • (1993) Nobel Lectures in Chemistry 1971-1980 , pp. 295-330
    • Mitchell, P.1
  • 5
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. and Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 8
    • 0034665878 scopus 로고    scopus 로고
    • Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms
    • Sazanov, L. A. and Walker, J. E. (2000) Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. J. Mol. Biol. 302, 455-464
    • (2000) J. Mol. Biol. , vol.302 , pp. 455-464
    • Sazanov, L.A.1    Walker, J.E.2
  • 9
    • 0036786230 scopus 로고    scopus 로고
    • The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: The role of aromatic-aromatic interaction in inhibition
    • Gao, X., Wen, X., Yu, C., Esser, L., Tsao, S., Quinn, B., Zhang, L., Yu, L. and Xia, D. (2002) The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition. Biochemistry 41, 11692-11702
    • (2002) Biochemistry , vol.41 , pp. 11692-11702
    • Gao, X.1    Wen, X.2    Yu, C.3    Esser, L.4    Tsao, S.5    Quinn, B.6    Zhang, L.7    Yu, L.8    Xia, D.9
  • 11
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • DOI 10.1038/nature02242
    • Osyczka, A., Moser, C. C., Daldal, F. and Dutton, P. L. (2004) Reversible redox energy coupling in electron transfer chains. Nature 427, 607-612 (Pubitemid 38248474)
    • (2004) Nature , vol.427 , Issue.6975 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 12
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein Complex II
    • DOI 10.1016/j.cell.2005.05.025, PII S0092867405005040
    • Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M. and Rao, Z. (2005) Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121, 1043-1057 (Pubitemid 40884395)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6    Bartlam, M.7    Rao, Z.8
  • 13
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex I
    • Efremov, R. G., Baradaran, R. and Sazanov, L. A. (2010) The architecture of respiratory complex I. Nature 465, 441-445
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 14
    • 79957707195 scopus 로고    scopus 로고
    • Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy
    • Marechal, A. and Rich, P. R. (2011) Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 108, 8634-8638
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 8634-8638
    • Marechal, A.1    Rich, P.R.2
  • 15
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex I
    • Efremov, R. G. and Sazanov, L. A. (2011) Structure of the membrane domain of respiratory complex I. Nature 476, 414-420
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 16
    • 0016853664 scopus 로고
    • A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport
    • Boyer, P. D. (1975) A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport. FEBS Lett. 58, 1-6
    • (1975) FEBS Lett. , vol.58 , pp. 1-6
    • Boyer, P.D.1
  • 17
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • DOI 10.1016/0005-2728(93)90063-L
    • Boyer, P. D. (1993) The binding change mechanism for ATP synthase: some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250 (Pubitemid 23015689)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1140 , Issue.3 , pp. 215-250
    • Boyer, P.D.1
  • 18
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J. P., Leslie, A. G. W., Lutter, R. and Walker, J. E. (1994) Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 19
    • 0010209746 scopus 로고    scopus 로고
    • ATP synthesis by rotary catalysis
    • Walker, J. E. (1998) ATP synthesis by rotary catalysis. Angew. Chem. Int. Ed. 37, 5000-5011
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 5000-5011
    • Walker, J.E.1
  • 20
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • DOI 10.1016/S0005-2728(96)00127-2, PII S0005272896001272
    • Dimroth, P. (1997) Primary sodium ion translocating enzymes. Biochim. Biophys. Acta 1318, 11-51 (Pubitemid 27051221)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1318 , Issue.1-2 , pp. 11-51
    • Dimroth, P.1
  • 21
    • 0037767525 scopus 로고    scopus 로고
    • o-ATP synthase from thermoalkaliphilic Bacillus sp. strain TA2.A1
    • DOI 10.1128/JB.185.15.4442-4449.2003
    • Cook, G. M., Keis, S., Morgan, H. W., von Ballmoos, C., Matthey, U., Kaim, G. and Dimroth, P. (2003) Purification and biochemical characterization of the F1Fo-ATP synthase from thermoalkaliphilic Bacillus sp. strain TA2. A1. J. Bacteriol. 185, 4442-4449 (Pubitemid 36890491)
    • (2003) Journal of Bacteriology , vol.185 , Issue.15 , pp. 4442-4449
    • Cook, G.M.1    Keis, S.2    Morgan, H.W.3    Von Ballmoos, C.4    Matthey, U.5    Kaim, G.6    Dimroth, P.7
  • 22
    • 0021829239 scopus 로고
    • 1-ATPase from bovine mitochondria
    • DOI 10.1016/0022-2836(85)90313-4
    • Walker, J. E., Fearnley, I. M., Gay, N. J., Gibson, B. W., Northrop, F. D., Powell, S. J., Runswick, M. J., Saraste, M. and Tybulewicz, V. L. (1985) Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria. J. Mol. Biol. 184, 677-701 (Pubitemid 15024774)
    • (1985) Journal of Molecular Biology , vol.184 , Issue.4 , pp. 677-701
    • Walker, J.E.1    Fearnley, I.M.2    Gay, N.J.3
  • 23
    • 0020375075 scopus 로고
    • 0 ATPases
    • DOI 10.1016/0014-5793(82)80960-5
    • Walker, J. E., Runswick, M. J. and Saraste, M. (1982) Subunit equivalence in Escherichia coli and bovine heart mitochondrial F1Fo-ATPases. FEBS Lett. 146, 393-396 (Pubitemid 13252928)
    • (1982) FEBS Letters , vol.146 , Issue.2 , pp. 393-396
    • Walker, J.E.1    Runswick, M.J.2    Saraste, M.3
  • 24
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A. G. and Walker, J. E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705 (Pubitemid 129515869)
    • (1999) Science , vol.286 , Issue.5445 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 28
    • 0032527132 scopus 로고    scopus 로고
    • 1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: The structure provides further support for a rotary catalytic mechanism
    • Orriss, G. L., Leslie, A. G. W., Braig, K. and Walker, J. E. (1998) Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. Structure 6, 831-837 (Pubitemid 28348646)
    • (1998) Structure , vol.6 , Issue.7 , pp. 831-837
    • Orriss, G.L.1    Leslie, A.G.W.2    Braig, K.3    Walker, J.E.4
  • 30
    • 0033766435 scopus 로고    scopus 로고
    • The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
    • Gibbons, C, Montgomery, M. G., Leslie, A. G. W. and Walker, J. E. (2000) The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution. Nat. Struct. Biol. 7, 1055-1061
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1055-1061
    • Gibbons, C.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 31
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • DOI 10.1016/S0092-8674(01)00452-4
    • Menz, R. I., Walker, J. E. and Leslie, A. G. W. (2001) Structure of bovine mitochondrial F1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106, 331-341 (Pubitemid 32772617)
    • (2001) Cell , vol.106 , Issue.3 , pp. 331-341
    • Menz R.Ian1    Walker, J.E.2    Leslie, A.G.W.3
  • 32
    • 0035815395 scopus 로고    scopus 로고
    • 1-ATPase are not influenced by crystallisation at high concentrations of nucleotide
    • DOI 10.1016/S0014-5793(01)02302-X, PII S001457930102302X
    • Menz, R. I., Leslie, A. G. W. and Walker, J. E. (2001) The structure and nucleotide occupancy of bovine mitochondrial F1-ATPase are not influenced by crystallisation at high concentrations of nucleotide. FEBS Lett. 494, 11-14 (Pubitemid 32289362)
    • (2001) FEBS Letters , vol.494 , Issue.1-2 , pp. 11-14
    • Menz R.Ian1    Leslie, A.G.W.2    Walker, J.E.3
  • 33
    • 3542996325 scopus 로고    scopus 로고
    • 1-ATPase inhibited by ADP and beryllium fluoride
    • DOI 10.1038/sj.emboj.7600293
    • Kagawa, R., Montgomery, M. G., Braig, K., Leslie, A. G. W. and Walker, J. E. (2004) The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride. EMBO J. 23, 2734-2744 (Pubitemid 39013546)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2734-2744
    • Kagawa, R.1    Montgomery, M.G.2    Braig, K.3    Leslie, A.G.W.4    Walker, J.E.5
  • 35
    • 34347226731 scopus 로고    scopus 로고
    • 1-ATPase from bovine heart mitochondria at 1.9 A resolution
    • DOI 10.1074/jbc.M700203200
    • Bowler, M. W., Montgomery, M. G., Leslie, A. G. W. and Walker, J. E. (2007) Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 Å resolution. J. Biol. Chem. 282, 14238-14242 (Pubitemid 47100445)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14238-14242
    • Bowler, M.W.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 38
    • 76049093135 scopus 로고    scopus 로고
    • The structure of the membrane extrinsic region of bovine ATP synthase
    • Rees, D. M., Leslie, A. G. W. and Walker, J. E. (2009) The structure of the membrane extrinsic region of bovine ATP synthase. Proc. Natl. Acad. Sci. U. S. A. 106, 21597-21601
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 21597-21601
    • Rees, D.M.1    Leslie, A.G.W.2    Walker, J.E.3
  • 39
    • 33751086144 scopus 로고    scopus 로고
    • 1 ATPase
    • DOI 10.1038/sj.emboj.7601410, PII 7601410
    • Kabaleeswaran, V., Puri, N., Walker, J. E., Leslie, A. G. W. and Mueller, D. M. (2006) Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase. EMBO J. 25, 5433-5442 (Pubitemid 44764152)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5433-5442
    • Kabaleeswaran, V.1    Puri, N.2    Walker, J.E.3    Leslie, A.G.W.4    Mueller, D.M.5
  • 41
    • 78449252457 scopus 로고    scopus 로고
    • Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncoupling
    • Arsenieva, D., Symersky, J., Wang, Y., Pagadala, V. and Mueller, D. M. (2010) Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncoupling. J. Biol. Chem. 285, 36561-36569
    • (2010) J. Biol. Chem. , vol.285 , pp. 36561-36569
    • Arsenieva, D.1    Symersky, J.2    Wang, Y.3    Pagadala, V.4    Mueller, D.M.5
  • 43
    • 77956552341 scopus 로고    scopus 로고
    • Crystal structure of the Mg-ADP-inhibited state of the yeast F1 c10-ATP synthase
    • Dautant, A., Velours, J. and Giraud, M. F. (2010) Crystal structure of the Mg-ADP-inhibited state of the yeast F1 c10-ATP synthase. J. Biol. Chem. 285, 29502-29510
    • (2010) J. Biol. Chem. , vol.285 , pp. 29502-29510
    • Dautant, A.1    Velours, J.2    Giraud, M.F.3
  • 44
    • 84863959033 scopus 로고    scopus 로고
    • Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
    • Rees, D. M., Montgomery, M. G., Leslie, A. G. W. and Walker, J. E. (2012) Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria. Proc. Natl. Acad. Sci. U. S. A. 109, 11139-11143
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 11139-11143
    • Rees, D.M.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 45
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji, H., Yasuda, R., Yoshida, M. and Kinosita, Jr, K. (1997) Direct observation of the rotation of F1-ATPase. Nature 386, 299-302
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr., K.4
  • 47
    • 0035912221 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1038/35073513
    • Yasuda, R., Noji, H., Yoshida, M., Kinosita, Jr, K. and Itoh, H. (2001) Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 410, 898-904 (Pubitemid 32335828)
    • (2001) Nature , vol.410 , Issue.6831 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita Jr., K.4    Itoh, H.5
  • 48
    • 57149107555 scopus 로고    scopus 로고
    • Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80° and 40° substep rotations
    • Masaike, T., Koyama-Horibe, F., Oiwa, K., Yoshida, M. and Nishizaka, T. (2008) Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80° and 40° substep rotations. Nat. Struct. Mol. Biol. 15, 1326-1333
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1326-1333
    • Masaike, T.1    Koyama-Horibe, F.2    Oiwa, K.3    Yoshida, M.4    Nishizaka, T.5
  • 49
    • 0021759513 scopus 로고
    • Role of a disulfide bond in the gamma subunit in activation of the ATPase of chloroplast coupling factor 1
    • Nalin, CM. and McCarty, R. E. (1984) Role of a disulfide bond in the gamma subunit in activation of the ATPase of chloroplast coupling factor 1. J. Biol. Chem. 259, 7275-7280
    • (1984) J. Biol. Chem. , vol.259 , pp. 7275-7280
    • Nalin, C.M.1    McCarty, R.E.2
  • 50
    • 0028588948 scopus 로고
    • The regulation of catalysis in ATP synthase
    • Walker, J. E. (1994) The regulation of catalysis in ATP synthase. Curr. Opin. Struct. Biol. 4, 912-918
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 912-918
    • Walker, J.E.1
  • 51
    • 0000228422 scopus 로고
    • A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity
    • Pullman, M. E. and Monroy, G. C. (1963) A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity. J. Biol. Chem. 238, 3762-3769
    • (1963) J. Biol. Chem. , vol.238 , pp. 3762-3769
    • Pullman, M.E.1    Monroy, G.C.2
  • 52
    • 0037126590 scopus 로고    scopus 로고
    • 1, the regulatory subunit of mitochondrial F-ATPase
    • DOI 10.1093/emboj/20.24.6990
    • Cabezon, E., Runswick, M. J., Leslie, A. G. W. and Walker, J. E. (2001) The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase. EMBOJ. 20, 6990-6996 (Pubitemid 34062291)
    • (2001) EMBO Journal , vol.20 , Issue.24 , pp. 6990-6996
    • Cabezon, E.1    Runswick, M.J.2    Leslie, A.G.W.3    Walker, J.E.4
  • 53
    • 0034664252 scopus 로고    scopus 로고
    • Dimerization of bovine F1-ATPase by binding the inhibitor protein, IF1. J
    • Cabezon, E., Arechaga, I., Jonathan, P., Butler, G. and Walker, J. E. (2000) Dimerization of bovine F1-ATPase by binding the inhibitor protein, IF1. J. Biol. Chem. 275, 28353-28355
    • (2000) Biol. Chem. , vol.275 , pp. 28353-28355
    • Cabezon, E.1    Arechaga, I.2    Jonathan, P.3    Butler, G.4    Walker, J.E.5
  • 54
    • 0034682781 scopus 로고    scopus 로고
    • Modulation of the oligomerization state of the bovine F1-ATPase inhibitor protein, IF1, by pH
    • Cabezon, E., Butler, P. J., Runswick, M. J. and Walker, J. E. (2000) Modulation of the oligomerization state of the bovine F1-ATPase inhibitor protein, IF1, by pH. J. Biol. Chem. 275, 25460-25464
    • (2000) J. Biol. Chem. , vol.275 , pp. 25460-25464
    • Cabezon, E.1    Butler, P.J.2    Runswick, M.J.3    Walker, J.E.4
  • 55
    • 79551682992 scopus 로고    scopus 로고
    • Binding of the inhibitor protein IF1 to bovine F1-ATPase
    • Bason, J. V., Runswick, M. J., Fearnley, I. M. and Walker, J. E. (2011) Binding of the inhibitor protein IF1 to bovine F1-ATPase. J. Mol. Biol. 406, 443-453
    • (2011) J. Mol. Biol. , vol.406 , pp. 443-453
    • Bason, J.V.1    Runswick, M.J.2    Fearnley, I.M.3    Walker, J.E.4
  • 58
    • 0018678906 scopus 로고
    • 1 ATPase
    • DOI 10.1016/0003-9861(79)90222-4
    • Laget, P. P. and Smith, J. B. (1979) Inhibitory properties of endogenous subunit s in the Escherichia coli F1 ATPase. Arch. Biochem. Biophys. 197, 83-89 (Pubitemid 10226710)
    • (1979) Archives of Biochemistry and Biophysics , vol.197 , Issue.1 , pp. 83-89
    • Laget, P.P.1    Smith, J.B.2
  • 60
    • 0032500380 scopus 로고    scopus 로고
    • 1-ATPase from Escherichia coli and interactions of this subunit with β subunits in the complex
    • DOI 10.1074/jbc.273.41.26645
    • Wilkens, S. and Capaldi, R. A. (1998) Solution structure of the s subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with f) subunits in the complex. J. Biol. Chem. 273, 26645-26651 (Pubitemid 28471678)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26645-26651
    • Wilkens, S.1    Capaldi, R.A.2
  • 61
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the y-s complex of ATP synthase
    • Rodgers, A. J. and Wilce, M. C. (2000) Structure of the y-s complex of ATP synthase. Nat. Struct. Biol. 7, 1051-1054
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.1    Wilce, M.C.2
  • 62
    • 79958858245 scopus 로고    scopus 로고
    • Structure of the ATP synthase catalytic complex F1 from Escherichia coli in an autoinhibited conformation
    • Cingolani, G. and Duncan, T. M. (2011) Structure of the ATP synthase catalytic complex F1 from Escherichia coli in an autoinhibited conformation. Nat. Struct. Mol. Biol. 18, 701-707
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 701-707
    • Cingolani, G.1    Duncan, T.M.2
  • 63
    • 78349253415 scopus 로고    scopus 로고
    • ATP synthase in slow-and fast-growing mycobacteria is active in ATP synthesis and blocked in ATP hydrolysis direction
    • Haagsma, A. C., Driessen, N. N., Hahn, M. M., Lill, H. and Bald, D. (2010) ATP synthase in slow-and fast-growing mycobacteria is active in ATP synthesis and blocked in ATP hydrolysis direction. FEMS Microbiol. Lett. 313, 68-74
    • (2010) FEMS Microbiol. Lett. , vol.313 , pp. 68-74
    • Haagsma, A.C.1    Driessen, N.N.2    Hahn, M.M.3    Lill, H.4    Bald, D.5
  • 64
    • 0028879404 scopus 로고
    • Correlations of structure and function in subunit c of Escherichia coli FoF1-ATP synthase
    • Fillingame, R. H., Girvin, M. E. and Zhang, Y. (1995) Correlations of structure and function in subunit c of Escherichia coli FoF1-ATP synthase. Biochem. Soc. Trans. 23, 760-766
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 760-766
    • Fillingame, R.H.1    Girvin, M.E.2    Zhang, Y.3
  • 65
    • 0032568818 scopus 로고    scopus 로고
    • 0 ATP synthase
    • DOI 10.1074/jbc.273.26.16241
    • Valiyaveetil, F. I. and Fillingame, R. H. (1998) Transmembrane topography of subunit a in the Escherichia coli F1 Fo ATP synthase. J. Biol. Chem. 273, 16241-16247 (Pubitemid 28311400)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16241-16247
    • Valiyaveetil, F.I.1    Fillingame, R.H.2
  • 66
    • 0024977998 scopus 로고
    • Proton translocation by the F1 Fo ATPase of Escherichia coli: Mutagenic analysis of the a subunit
    • Cain, B. D. and Simoni, R. D. (1989) Proton translocation by the F1 Fo ATPase of Escherichia coli: mutagenic analysis of the a subunit. J. Biol. Chem. 264, 3292-3300
    • (1989) J. Biol. Chem. , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 68
    • 34247877574 scopus 로고    scopus 로고
    • Aqueous access pathways in ATP synthase subunit a: Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5
    • DOI 10.1074/jbc.M610848200
    • Angevine, CM., Herold, K. A., Vincent, O. D. and Fillingame, R. H. (2007) Aqueous access pathways in ATP synthase subunit a: reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. J. Biol. Chem. 282, 9001-9007 (Pubitemid 47093514)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 9001-9007
    • Angevine, C.M.1    Herold, K.A.G.2    Vincent, O.D.3    Fillingame, R.H.4
  • 69
    • 84863242790 scopus 로고    scopus 로고
    • Functional analysis of membranous Fo: A subunit of F1Fo-ATP synthase by in vitro protein synthesis
    • Kuruma, Y., Suzuki, T., Ono, S., Yoshida, M. and Ueda, T. (2012) Functional analysis of membranous Fo: a subunit of F1Fo-ATP synthase by in vitro protein synthesis. Biochem. J. 442, 631-638
    • (2012) Biochem. J. , vol.442 , pp. 631-638
    • Kuruma, Y.1    Suzuki, T.2    Ono, S.3    Yoshida, M.4    Ueda, T.5
  • 70
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • DOI 10.1016/j.bbabio.2006.01.001, PII S0005272806000028
    • Walker, J. E. and Dickson, V. K. (2006) The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 1757, 286-296 (Pubitemid 43996944)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 72
    • 33947585115 scopus 로고    scopus 로고
    • o-ATP Synthase Interacts with the N-terminal Region of an Alpha Subunit
    • DOI 10.1016/j.jmb.2007.02.059, PII S0022283607002409
    • Carbajo, R. J., Kellas, F. A., Yang, J. C, Runswick, M. J., Montgomery, M. G., Walker, J. E. and Neuhaus, D. (2007) How the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an a subunit. J. Mol. Biol. 368, 310-318 (Pubitemid 46483497)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 310-318
    • Carbajo, R.J.1    Kellas, F.A.2    Yang, J.-C.3    Runswick, M.J.4    Montgomery, M.G.5    Walker, J.E.6    Neuhaus, D.7
  • 73
    • 0027943885 scopus 로고
    • ATP synthase from bovine heart mitochondria: In vitro assembly of a stalk complex in the presence of F1-ATPase and in its absence
    • Collinson, I. R., van Raaij, M. J., Runswick, M. J., Fearnley, I. M., Skehel, J. M., Orriss, G. L, Miroux, B. and Walker, J. E. (1994) ATP synthase from bovine heart mitochondria: in vitro assembly of a stalk complex in the presence of F1-ATPase and in its absence. J. Mol. Biol. 242, 408-421
    • (1994) J. Mol. Biol. , vol.242 , pp. 408-421
    • Collinson, I.R.1    Van Raaij, M.J.2    Runswick, M.J.3    Fearnley, I.M.4    Skehel, J.M.5    Orriss, G.L.6    Miroux, B.7    Walker, J.E.8
  • 74
    • 4344715981 scopus 로고    scopus 로고
    • 6 from the peripheral stalk region of ATP synthase from bovine heart mitochondria
    • DOI 10.1016/j.jmb.2004.07.013, PII S002228360400823X
    • Carbajo, R. J., Silvester, J. A., Runswick, M. J., Walker, J. E. and Neuhaus, D. (2004) Solution structure of subunit F6 from the peripheral stalk region of ATP synthase from bovine heart mitochondria. J. Mol. Biol. 342, 593-603 (Pubitemid 39149761)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 593-603
    • Carbajo, R.J.1    Silvester, J.A.2    Runswick, M.J.3    Walker, J.E.4    Neuhaus, D.5
  • 75
    • 0036971192 scopus 로고    scopus 로고
    • ATP synthase from Saccharomyces cerevisiae: Location of the OSCP subunit in the peripheral stalk region
    • DOI 10.1016/S0022-2836(02)00671-X
    • Rubinstein, J. L. and Walker, J. E. (2002) ATP synthase from Saccharomyces cerevisiae: location of the OSCP subunit in the peripheral stalk region. J. Mol. Biol. 321, 613-619 (Pubitemid 36124800)
    • (2002) Journal of Molecular Biology , vol.321 , Issue.4 , pp. 613-619
    • Rubinstein, J.L.1    Walker, J.E.2
  • 76
    • 9644265246 scopus 로고    scopus 로고
    • ATP synthase from Saccharomyces cerevisiae: Location of subunit h in the peripheral stalk region
    • DOI 10.1016/j.jmb.2004.10.060, PII S0022283604013658
    • Rubinstein, J. L., Dickson, V. K., Runswick, M. J. and Walker, J. E. (2005) ATP synthase from Saccharomyces cerevisiae: location of subunit h in the peripheral stalk region. J. Mol. Biol. 345, 513-520 (Pubitemid 39575921)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.3 , pp. 513-520
    • Rubinstein, J.L.1    Dickson, V.K.2    Runswick, M.J.3    Walker, J.E.4
  • 77
    • 33745548556 scopus 로고    scopus 로고
    • On the structure of the stator of the mitochondrial ATP synthase
    • DOI 10.1038/sj.emboj.7601177, PII 7601177
    • Dickson, V. K., Silvester, J. A., Fearnley, I. M., Leslie, A. G. W. and Walker, J. E. (2006) On the structure of the stator of the mitochondrial ATP synthase. EMBO J. 25, 2911-2918 (Pubitemid 43980397)
    • (2006) EMBO Journal , vol.25 , Issue.12 , pp. 2911-2918
    • Dickson, V.K.1    Silvester, J.A.2    Fearnley, I.M.3    Leslie, A.G.W.4    Walker, J.E.5
  • 78
    • 0031055743 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the δ subunit of the E. coli ATPsynthase
    • DOI 10.1038/nsb0397-198
    • Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F. W. and Capaldi, R. A. (1997) Solution structure of the N-terminal domain of the d subunit of the E. coli ATP synthase. Nat. Struct. Biol. 4, 198-201 (Pubitemid 27114629)
    • (1997) Nature Structural Biology , vol.4 , Issue.3 , pp. 198-201
    • Wilkens, S.1    Dunn, S.D.2    Chandler, J.3    Dahlquist, F.W.4    Capaldi, R.A.5
  • 79
    • 0034695406 scopus 로고    scopus 로고
    • Localization of the d subunit in the Escherichia coli F1Fo-ATPsynthase by immuno electron microscopy: The d subunit binds on top of the F1
    • Wilkens, S., Zhou, J., Nakayama, R., Dunn, S. D. and Capaldi, R. A. (2000) Localization of the d subunit in the Escherichia coli F1Fo-ATPsynthase by immuno electron microscopy: the d subunit binds on top of the F1. J. Mol. Biol. 295, 387-391
    • (2000) J. Mol. Biol. , vol.295 , pp. 387-391
    • Wilkens, S.1    Zhou, J.2    Nakayama, R.3    Dunn, S.D.4    Capaldi, R.A.5
  • 80
    • 0023645444 scopus 로고
    • ATP synthase from bovine mitochondria: The characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs
    • Walker, J. E., Runswick, M. J. and Poulter, L. (1987) ATP synthase from bovine mitochondria: the characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs. J. Mol. Biol. 197, 89-100
    • (1987) J. Mol. Biol. , vol.197 , pp. 89-100
    • Walker, J.E.1    Runswick, M.J.2    Poulter, L.3
  • 81
    • 33750951013 scopus 로고    scopus 로고
    • ATP Synthase b Subunit Dimerization Domain: A Right-Handed Coiled Coil with Offset Helices
    • DOI 10.1016/j.jmb.2006.09.028, PII S0022283606012198
    • Del Rizzo, P. A., Bi, Y. and Dunn, S. D. (2006) ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices. J. Mol. Biol. 364, 735-746 (Pubitemid 44737827)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.4 , pp. 735-746
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3
  • 82
    • 45849087668 scopus 로고    scopus 로고
    • Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils
    • Wise, J. G. and Vogel, P. D. (2008) Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils. Biophys. J. 94, 5040-5052
    • (2008) Biophys. J. , vol.94 , pp. 5040-5052
    • Wise, J.G.1    Vogel, P.D.2
  • 83
    • 0032983519 scopus 로고    scopus 로고
    • Structure of the membrane domain of subunit b of the Escherichia coli FoF1 ATP synthase
    • Dmitriev, O., Jones, P. C., Jiang, W. and Fillingame, R. H. (1999) Structure of the membrane domain of subunit b of the Escherichia coli FoF1 ATP synthase. J. Biol. Chem. 274, 15598-15604
    • (1999) J. Biol. Chem. , vol.274 , pp. 15598-15604
    • Dmitriev, O.1    Jones, P.C.2    Jiang, W.3    Fillingame, R.H.4
  • 84
    • 4043052974 scopus 로고    scopus 로고
    • 2-subunits as an anchor rail of a rotating c-ring
    • DOI 10.1074/jbc.M404993200
    • Ono, S., Sone, N., Yoshida, M. and Suzuki, T. (2004) ATP synthase that lacks Fo a-subunit: isolation, properties, and indication of Fo b2-subunits as an anchor rail of a rotating c-ring. J. Biol. Chem. 279, 33409-33412 (Pubitemid 39062989)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33409-33412
    • Ono, S.1    Sone, N.2    Yoshida, M.3    Suzuki, T.4
  • 85
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • DOI 10.1016/S0014-5793(99)00386-5, PII S0014579399003865
    • Cherepanov, D. A., Mulkidjanian, A. Y. and Junge, W. (1999) Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Lett. 449, 1-6 (Pubitemid 29182659)
    • (1999) FEBS Letters , vol.449 , Issue.1 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 87
    • 0036073866 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1016/S0969-2126(02)00789-X, PII S096921260200789X
    • Ma, J., Flynn, T. C., Cui, Q., Leslie, A. G., Walker, J. E. and Karplus, M. (2002) A dynamic analysis of the rotation mechanism for conformational change in F1-ATPase. Structure 10, 921-931 (Pubitemid 34786737)
    • (2002) Structure , vol.10 , Issue.7 , pp. 921-931
    • Ma, J.1    Flynn, T.C.2    Cui, Q.3    Leslie, A.G.W.4    Walker, J.E.5    Karplus, M.6
  • 89
    • 64649086247 scopus 로고    scopus 로고
    • The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region
    • Matthies, D., Preiss, L., Klyszejko, A. L., Muller, D. J., Cook, G. M., Vonck, J. and Meier, T. (2009) The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region. J. Mol. Biol. 388, 611-618
    • (2009) J. Mol. Biol. , vol.388 , pp. 611-618
    • Matthies, D.1    Preiss, L.2    Klyszejko, A.L.3    Muller, D.J.4    Cook, G.M.5    Vonck, J.6    Meier, T.7
  • 90
    • 67650546998 scopus 로고    scopus 로고
    • Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase
    • Vollmar, M., Schlieper, D., Winn, M., Buchner, C. and Groth, G. (2009) Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase. J. Biol. Chem. 284, 18228-18235
    • (2009) J. Biol. Chem. , vol.284 , pp. 18228-18235
    • Vollmar, M.1    Schlieper, D.2    Winn, M.3    Buchner, C.4    Groth, G.5
  • 91
    • 70349828967 scopus 로고    scopus 로고
    • High-resolution structure of the rotor ring of a proton-dependent ATP synthase
    • Pogoryelov, D., Yildiz, O., Faraldo-Gomez, J. D. and Meier, T. (2009) High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat. Struct. Mol. Biol. 16, 1068-1073
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1068-1073
    • Pogoryelov, D.1    Yildiz, O.2    Faraldo-Gomez, J.D.3    Meier, T.4
  • 92
    • 11144263646 scopus 로고    scopus 로고
    • P/O ratios of mitochondrial oxidative phosphorylation
    • DOI 10.1016/j.bbabio.2004.09.004, PII S0005272804002701
    • Hinkle, P. C. (2005) P/O ratios of mitochondrial oxidative phosphorylation. Biochim. Biophys. Acta 1706, 1-11 (Pubitemid 40037758)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 1-11
    • Hinkle, P.C.1
  • 93
    • 77049233362 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization
    • Chance, B. and Williams, G. R. (1955) Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization. J. Biol. Chem. 217, 383-393
    • (1955) J. Biol. Chem. , vol.217 , pp. 383-393
    • Chance, B.1    Williams, G.R.2
  • 94
    • 0025923549 scopus 로고
    • Identification of the subunits of F1Fo-ATPase from bovine heart mitochondria
    • Walker, J. E., Lutter, R., Dupuis, A. and Runswick, M. J. (1991) Identification of the subunits of F1Fo-ATPase from bovine heart mitochondria. Biochemistry 30, 5369-5378
    • (1991) Biochemistry , vol.30 , pp. 5369-5378
    • Walker, J.E.1    Lutter, R.2    Dupuis, A.3    Runswick, M.J.4
  • 95
    • 0028181140 scopus 로고
    • Fo membrane domain of ATP synthase from bovine heart mitochondria: Purification, subunit composition, and reconstitution with F1-ATPase
    • Collinson, I. R., Runswick, M. J., Buchanan, S. K., Fearnley, I. M., Skehel, J. M., van Raaij, M. J., Griffiths, D. E. and Walker, J. E. (1994) Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase. Biochemistry 33, 7971-7978
    • (1994) Biochemistry , vol.33 , pp. 7971-7978
    • Collinson, I.R.1    Runswick, M.J.2    Buchanan, S.K.3    Fearnley, I.M.4    Skehel, J.M.5    Van Raaij, M.J.6    Griffiths, D.E.7    Walker, J.E.8
  • 96
    • 0022760932 scopus 로고
    • Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase
    • Fearnley, I. M. and Walker, J. E. (1986) Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase. EMBO J. 5, 2003-2008
    • (1986) EMBO J. , vol.5 , pp. 2003-2008
    • Fearnley, I.M.1    Walker, J.E.2
  • 97
    • 34250886311 scopus 로고    scopus 로고
    • Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria
    • DOI 10.1016/j.febslet.2007.05.079, PII S001457930700631X
    • Chen, R., Runswick, M. J., Carroll, J., Fearnley, I. M. and Walker, J. E. (2007) Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria. FEBS Lett. 581, 3145-3148 (Pubitemid 46977353)
    • (2007) FEBS Letters , vol.581 , Issue.17 , pp. 3145-3148
    • Chen, R.1    Runswick, M.J.2    Carroll, J.3    Fearnley, I.M.4    Walker, J.E.5
  • 98
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • DOI 10.1093/emboj/cdg608
    • Rubinstein, J. L., Walker, J. E. and Henderson, R. (2003) Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J. 22, 6182-6192 (Pubitemid 37522576)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 99
    • 51349153212 scopus 로고    scopus 로고
    • Cryo-EM structure of the yeast ATP synthase
    • Lau, W. C. Y., Baker, L. A. and Rubinstein, J. L. (2008) Cryo-EM structure of the yeast ATP synthase. J. Mol. Biol. 382, 1256-1264
    • (2008) J. Mol. Biol. , vol.382 , pp. 1256-1264
    • Lau, W.C.Y.1    Baker, L.A.2    Rubinstein, J.L.3
  • 100
  • 104
    • 56649096812 scopus 로고    scopus 로고
    • Functional halt positions of rotary F1Fo-ATPase correlated with crystal structures
    • Sielaff, H., Rennekamp, H., Engelbrecht, S. and Junge, W. (2008) Functional halt positions of rotary F1Fo-ATPase correlated with crystal structures. Biophys. J. 95, 4979-4987
    • (2008) Biophys. J. , vol.95 , pp. 4979-4987
    • Sielaff, H.1    Rennekamp, H.2    Engelbrecht, S.3    Junge, W.4
  • 105
    • 50949098032 scopus 로고    scopus 로고
    • Structural organization of mitochondrial ATP synthase
    • Wittig, I. and Schagger, H. (2008) Structural organization of mitochondrial ATP synthase. Biochim. Biophys. Acta 1777, 592-598
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 592-598
    • Wittig, I.1    Schagger, H.2
  • 106
    • 77953130160 scopus 로고    scopus 로고
    • Imaging of organelles by electron microscopy reveals protein-protein interactions in mitochondria and chloroplasts
    • Dudkina, N. V., Kouril, R., Bultema, J. B. and Boekema, E. J. (2010) Imaging of organelles by electron microscopy reveals protein-protein interactions in mitochondria and chloroplasts. FEBS Lett. 584, 2510-2515
    • (2010) FEBS Lett. , vol.584 , pp. 2510-2515
    • Dudkina, N.V.1    Kouril, R.2    Bultema, J.B.3    Boekema, E.J.4
  • 107
    • 79955396906 scopus 로고    scopus 로고
    • Electron tomography of plant thylakoid membranes
    • Daum, B. and Kuhlbrandt, W. (2011) Electron tomography of plant thylakoid membranes. J. Exp. Bot. 62, 2393-2402
    • (2011) J. Exp. Bot. , vol.62 , pp. 2393-2402
    • Daum, B.1    Kuhlbrandt, W.2
  • 108
  • 109
    • 26844548023 scopus 로고    scopus 로고
    • Structure of dimeric ATP synthase from mitochondria: An angular association of monomers induces the strong curvature of the inner membrane
    • DOI 10.1016/j.febslet.2005.09.065, PII S001457930501183X
    • Dudkina, N. V., Heinemeyer, J., Keegstra, W., Boekema, E. J. and Braun H. P. (2005) Structure of dimeric ATP synthase from mitochondria: an angular association of monomers induces the strong curvature of the inner membrane. FEBS Lett. 579, 5769-5772 (Pubitemid 41455662)
    • (2005) FEBS Letters , vol.579 , Issue.25 , pp. 5769-5772
    • Dudkina, N.V.1    Heinemeyer, J.2    Keegstra, W.3    Boekema, E.J.4    Braun, H.-P.5
  • 110
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • DOI 10.1038/emboj.2008.35, PII EMBOJ200835
    • Strauss, M., Hofhaus, G., Schroder, R. R. and Kuhlbrandt, W. (2008) Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 27, 1154-1160 (Pubitemid 351508145)
    • (2008) EMBO Journal , vol.27 , Issue.7 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schroder, R.R.3    Kuhlbrandt, W.4
  • 111
    • 73249153664 scopus 로고    scopus 로고
    • Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography
    • Dudkina, N. V., Oostergetel, G. T., Lewejohann, D., Braun, H. P. and Boekema, E. J. (2010) Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography. Biochim. Biophys. Acta 1797, 272-277
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 272-277
    • Dudkina, N.V.1    Oostergetel, G.T.2    Lewejohann, D.3    Braun, H.P.4    Boekema, E.J.5
  • 113
    • 0343964750 scopus 로고
    • 31P nuclear magnetic resonance spectroscopy
    • Eble, K. S., Coleman, W. B., Hantgan, R. R. and Cunningham, C. C. (1990) Tightly associated cardiolipin in the bovine heart mitochondrial ATP synthase as analyzed by 31P nuclear magnetic resonance spectroscopy. J. Biol. Chem. 265, 19434-19440 (Pubitemid 120013882)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.32 , pp. 19434-19440
    • Eble, K.S.1    Coleman, W.B.2    Hantgan, R.R.3    Cunningham, C.C.4
  • 114
    • 2542447058 scopus 로고    scopus 로고
    • Lysine 43 is trimethylated in subunit c from bovine mitochondrial ATP synthase and in storage bodies associated with Batten disease
    • DOI 10.1074/jbc.M402074200
    • Chen, R., Fearnley, I. M., Palmer, D. N. and Walker, J. E. (2004) Lysine 43 is trimethylated in subunit c from bovine mitochondrial ATP synthase and in storage bodies associated with Batten disease. J. Biol. Chem. 279, 21883-21887 (Pubitemid 38679377)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 21883-21887
    • Chen, R.1    Fearnley, I.M.2    Palmer, D.N.3    Walker, J.E.4
  • 116
    • 0018399751 scopus 로고
    • Asymmetric distribution of phospholipids in the inner membrane of beef heart mitochondria
    • Krebs, J. J., Hauser, H. and Carafoli, E. (1979) Asymmetric distribution of phospholipids in the inner membrane of beef heart mitochondria. J. Biol. Chem. 254, 5308-5316 (Pubitemid 9227483)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.12 , pp. 5308-5316
    • Krebs, J.J.R.1    Hauser, H.2    Carafoli, E.3
  • 117
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?
    • DOI 10.1016/S0005-2736(96)00240-4, PII S0005273696002404
    • de Kroon, A. I., Dolis, D., Mayer, A., Lill, R. and de Kruijff, B. (1997) Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa: is cardiolipin present in the mitochondrial outer membrane? Biochim. Biophys. Acta 1325, 108-116 (Pubitemid 27138481)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1325 , Issue.1 , pp. 108-116
    • De Kroon, A.I.P.M.1    Dolis, D.2    Mayer, A.3    Lill, R.4    De Kruijff, B.5
  • 118
    • 77952216490 scopus 로고    scopus 로고
    • Macromolecules that prefer their membranes curvy
    • Huang, K. C. and Ramamurthi, K. S. (2010) Macromolecules that prefer their membranes curvy. Mol. Microbiol. 76, 822-832
    • (2010) Mol. Microbiol. , vol.76 , pp. 822-832
    • Huang, K.C.1    Ramamurthi, K.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.