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Volumn 57, Issue 3, 1998, Pages 253-266

Nucleotide-CF1 interactions and current views on the catalytic mechanism

Author keywords

Activation of catalytic properties; Binding change; Mechanism; Regulatory sites; Role of magnesium; Tentoxin

Indexed keywords


EID: 0031772039     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006034231713     Document Type: Article
Times cited : (3)

References (100)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Angstrom of F1-ATPase from bovine heart mitochondria
    • Abrahams J, Leslie A, Lutter R and Walker J (1994) Structure at 2.8 Angstrom of F1-ATPase from bovine heart mitochondria. Nature 370: 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.1    Leslie, A.2    Lutter, R.3    Walker, J.4
  • 2
    • 0017806139 scopus 로고
    • Kinetic mechanisms of ionic activation and inhibition of the adenosine triphosphatase of the 13 S coupling factor of oxydative phosphorylation
    • Adolfsen R and Moudrianakis E (1978) Kinetic mechanisms of ionic activation and inhibition of the adenosine triphosphatase of the 13 S coupling factor of oxydative phosphorylation. J Biol Chem 253: 4380-4388
    • (1978) J Biol Chem , vol.253 , pp. 4380-4388
    • Adolfsen, R.1    Moudrianakis, E.2
  • 3
    • 0029889206 scopus 로고    scopus 로고
    • Nucleotide-dependent movement of the f subunit between a and subunits in the Escherichia coli F1F0-type ATPase
    • Aggeler R and Capaldi R (1996) Nucleotide-dependent movement of the f subunit between a and subunits in the Escherichia coli F1F0-type ATPase. J Biol Chem 271: 13888-13891
    • (1996) J Biol Chem , vol.271 , pp. 13888-13891
    • Aggeler, R.1    Capaldi, R.2
  • 4
    • 0001103440 scopus 로고
    • Effect of methanol on spinach thylakoid ATPase
    • Anthon G and Jagendorf A (1983) Effect of methanol on spinach thylakoid ATPase. Biochim Biophys Acta 723: 358-365
    • (1983) Biochim Biophys Acta , vol.723 , pp. 358-365
    • Anthon, G.1    Jagendorf, A.2
  • 5
    • 0026785393 scopus 로고
    • Tentoxin sensitivity of chloroplasts determined by codon 83 of β subunit of proton-ATPase
    • Avni A, Anderson J, Holland N, Rochaix J-D, Gromet-Elhanan Z and Edelman M (1992) Tentoxin sensitivity of chloroplasts determined by codon 83 of β subunit of proton-ATPase. Science 257: 1245-1247
    • (1992) Science , vol.257 , pp. 1245-1247
    • Avni, A.1    Anderson, J.2    Holland, N.3    Rochaix, J.-D.4    Gromet-Elhanan, Z.5    Edelman, M.6
  • 6
    • 0026433426 scopus 로고
    • Hydrolysis of ATP by F1 can be described only on the basis of a dual-site mechanism
    • Berden J, Hartog A, Edel C (1991) Hydrolysis of ATP by F1 can be described only on the basis of a dual-site mechanism. Biochim Biophys Acta 1057: 151-156
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 151-156
    • Berden, J.1    Hartog, A.2    Edel, C.3
  • 7
    • 0028175791 scopus 로고
    • 2+ in the hydrolytic activity of the isolated chloroplast ATPase: Study by high-performance liquid chromatography
    • 2+ in the hydrolytic activity of the isolated chloroplast ATPase: Study by high-performance liquid chromatography. J Bioenerg Biomembr 26: 335-346
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 335-346
    • Berger, G.1    Girault, G.2    Galmiche, J.-M.3    Pezennec, S.4
  • 8
    • 4243656979 scopus 로고
    • Characterization of nucleotide binding sites on membrane-bound chloroplast ATPase by modification with pyridoxal 5′-phosphate
    • Bickel-Sandkötter S and Gokus M (1989) Characterization of nucleotide binding sites on membrane-bound chloroplast ATPase by modification with pyridoxal 5′-phosphate. Biochim Biophys Acta 974: 30-35
    • (1989) Biochim Biophys Acta , vol.974 , pp. 30-35
    • Bickel-Sandkötter, S.1    Gokus, M.2
  • 10
    • 0019889787 scopus 로고
    • Further characterization of nucleotide binding sites on chloroplast coupling factor one
    • Bruist M and Hammes G (1981) Further characterization of nucleotide binding sites on chloroplast coupling factor one. Biochemistry 20: 6298-6305
    • (1981) Biochemistry , vol.20 , pp. 6298-6305
    • Bruist, M.1    Hammes, G.2
  • 11
    • 0023664843 scopus 로고
    • Evidence for functional heterogeneity among the catalytic sites of the bovine heart mitochondrial Fl-ATPase
    • Bullough D, Verburg J, Yoshida M and Allison W (1987) Evidence for functional heterogeneity among the catalytic sites of the bovine heart mitochondrial Fl-ATPase. J Biol Chem 262: 11675-11683
    • (1987) J Biol Chem , vol.262 , pp. 11675-11683
    • Bullough, D.1    Verburg, J.2    Yoshida, M.3    Allison, W.4
  • 13
    • 0029764323 scopus 로고    scopus 로고
    • +-ATPase from chloroplast and Bacillus PS3 studied by EPR and pulsed EPR spectroscopy of bound manganese (II)
    • +-ATPase from chloroplast and Bacillus PS3 studied by EPR and pulsed EPR spectroscopy of bound manganese (II). Biochemistry 35: 9880-9891
    • (1996) Biochemistry , vol.35 , pp. 9880-9891
    • Buy, C.1    Girault, G.2    Zimmermann, J.-L.3
  • 14
    • 0029804181 scopus 로고    scopus 로고
    • 3γ subcomplex studied by one-dimensional ESEEM and two-dimensional HYSCORE spectroscopy of oxovanadium(IV) complexes: A possible role for β-His-324
    • 3γ subcomplex studied by one-dimensional ESEEM and two-dimensional HYSCORE spectroscopy of oxovanadium(IV) complexes: A possible role for β-His-324. Biochemistry 35: 14281-14293
    • (1996) Biochemistry , vol.35 , pp. 14281-14293
    • Buy, C.1    Matsui, T.2    Andrianambinintsoa, S.3    Sigalat, C.4    Girault, G.5    Zimmermann, J.-L.6
  • 15
    • 33646322622 scopus 로고
    • Structural changes of CF1-ATPase in solution
    • Calmettes P, Pezennec S, Berger G and Girault G (1992) Structural changes of CF1-ATPase in solution. Physica B 180 and 181: 765-766
    • (1992) Physica B , vol.180-181 , pp. 765-766
    • Calmettes, P.1    Pezennec, S.2    Berger, G.3    Girault, G.4
  • 16
    • 0029055549 scopus 로고
    • New synthesis of the cyclic tetrapeptide tentoxin employing an azlactone as key intermediate
    • Cavelier C and Verducci J (1995) New synthesis of the cyclic tetrapeptide tentoxin employing an azlactone as key intermediate. Tetrahedron Lett 36: 4425-4428
    • (1995) Tetrahedron Lett , vol.36 , pp. 4425-4428
    • Cavelier, C.1    Verducci, J.2
  • 17
    • 0027970292 scopus 로고
    • Chloroplast molecular chaperone-assisted refolding and reconstitution of an active multisubunit coupling factor CF1 core
    • Chen G and Jagendorf A (1994) Chloroplast molecular chaperone-assisted refolding and reconstitution of an active multisubunit coupling factor CF1 core. Proc Natl Acad Sci USA 91: 11497-11501
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11497-11501
    • Chen, G.1    Jagendorf, A.2
  • 18
    • 0018800270 scopus 로고
    • Occurrence and significance of oxygen exchange reactions catalyzed by mitochondrial adenosine triphosphatase preparations
    • Choate G, Hutton R and Boyer P (1979) Occurrence and significance of oxygen exchange reactions catalyzed by mitochondrial adenosine triphosphatase preparations. J Biol Chem 254: 286-290
    • (1979) J Biol Chem , vol.254 , pp. 286-290
    • Choate, G.1    Hutton, R.2    Boyer, P.3
  • 19
    • 0029162512 scopus 로고
    • Influence of nucleotides on the secondary structure and on the thermal stability of mitochondrial F1 visualized by infrared spectroscopy
    • Cladera J, Villaverde J, Hartog F, Padros E, Berden J, Rigaud J-L, Dunach M (1995) Influence of nucleotides on the secondary structure and on the thermal stability of mitochondrial F1 visualized by infrared spectroscopy. FEBS Lett 371: 115-118
    • (1995) FEBS Lett , vol.371 , pp. 115-118
    • Cladera, J.1    Villaverde, J.2    Hartog, F.3    Padros, E.4    Berden, J.5    Rigaud, J.-L.6    Dunach, M.7
  • 20
    • 0024062964 scopus 로고
    • The number of functional catalytic sites on F1-ATPases and the effect of quaternary structural asymmetry on their properties
    • Cross R (1988) The number of functional catalytic sites on F1-ATPases and the effect of quaternary structural asymmetry on their properties. J Bioenerg Biomemb 20: 395-405
    • (1988) J Bioenerg Biomemb , vol.20 , pp. 395-405
    • Cross, R.1
  • 21
    • 0020491221 scopus 로고
    • Mechanism of ATP hydrolysis by beef-heart mitochondrial ATPase
    • Cross R, Grubmeyer C and Penefsky H (1982) Mechanism of ATP hydrolysis by beef-heart mitochondrial ATPase. J Biol Chem 257: 12101-12105
    • (1982) J Biol Chem , vol.257 , pp. 12101-12105
    • Cross, R.1    Grubmeyer, C.2    Penefsky, H.3
  • 23
    • 0029810877 scopus 로고    scopus 로고
    • Differences between two tight ADP binding sites of the chloroplast coupling factor 1 and their effects on ATPase activity
    • Digel J, Kishinevsky A, Ong A and MC Carty R (1996) Differences between two tight ADP binding sites of the chloroplast coupling factor 1 and their effects on ATPase activity. J Biol Chem 271: 19976-19982
    • (1996) J Biol Chem , vol.271 , pp. 19976-19982
    • Digel, J.1    Kishinevsky, A.2    Ong, A.3    Carty R, M.C.4
  • 24
    • 0019320447 scopus 로고
    • Hysteretic' behavior and nucleotide binding sites of pig heart mitochondrial F1 adenosine 5′-triphosphatase
    • Di Pietro A, Penin F, Godinot C and Gautheron D (1980) 'Hysteretic' behavior and nucleotide binding sites of pig heart mitochondrial F1 adenosine 5′-triphosphatase. Biochemistry 19: 5671-5678
    • (1980) Biochemistry , vol.19 , pp. 5671-5678
    • Di Pietro, A.1    Penin, F.2    Godinot, C.3    Gautheron, D.4
  • 25
    • 0019889785 scopus 로고
    • Interaction between catalytic and regulatory sites of mitochondrial F1 adenosine-5′-triphosphatase
    • Di Pietro A, Godinot C, Gautheron D (1981) Interaction between catalytic and regulatory sites of mitochondrial F1 adenosine-5′-triphosphatase. Biochemistry 20: 6312-6318
    • (1981) Biochemistry , vol.20 , pp. 6312-6318
    • Di Pietro, A.1    Godinot, C.2    Gautheron, D.3
  • 27
    • 0000539715 scopus 로고
    • A survey of plant insensitivity to tentoxin
    • Durbin R and Uchytil T (1977) A survey of plant insensitivity to tentoxin. Phytopathology 67: 602-603
    • (1977) Phytopathology , vol.67 , pp. 602-603
    • Durbin, R.1    Uchytil, T.2
  • 28
    • 0025139058 scopus 로고
    • +-ATPases: At the interface between proton flow and ATP synthesis
    • +-ATPases: At the interface between proton flow and ATP synthesis. Biochim Biophys Acta 1015: 379-390
    • (1990) Biochim Biophys Acta , vol.1015 , pp. 379-390
    • Engelbrecht, S.1    Junge, W.2
  • 29
    • 0024969394 scopus 로고
    • Chloroplast ATP synthase contains one single copy of subunit S that is indispensable for photophosphorylation
    • Engelbrecht S, Schürmann K and Junge W (1989) Chloroplast ATP synthase contains one single copy of subunit S that is indispensable for photophosphorylation. Eur J Biochem 117-122
    • (1989) Eur J Biochem , pp. 117-122
    • Engelbrecht, S.1    Schürmann, K.2    Junge, W.3
  • 30
    • 0014949426 scopus 로고
    • Studies on the mechanism of the conversion of coupling factor 1 from chloroplasts to an active adenosine triphosphatase
    • Farron F and Racker E (1970) Studies on the mechanism of the conversion of coupling factor 1 from chloroplasts to an active adenosine triphosphatase. Biochemistry 19: 3829-3836
    • (1970) Biochemistry , vol.19 , pp. 3829-3836
    • Farron, F.1    Racker, E.2
  • 31
    • 0020490369 scopus 로고
    • The synthesis of enzyme-bound ATP by soluble chloroplast coupling factor 1
    • Feldman R and Sigman D (1982) The synthesis of enzyme-bound ATP by soluble chloroplast coupling factor 1. J Biol Chem 257: 1676-1683
    • (1982) J Biol Chem , vol.257 , pp. 1676-1683
    • Feldman, R.1    Sigman, D.2
  • 32
    • 0025165464 scopus 로고
    • ATP-hydrolysis in chloropasts: Unisite catalysis and evidence for heterogeneity of catalytic sites
    • Fromme P and Gräber P (1990) ATP-hydrolysis in chloropasts: Unisite catalysis and evidence for heterogeneity of catalytic sites. Biochim Biophys Acta 1020: 187-194
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 187-194
    • Fromme, P.1    Gräber, P.2
  • 33
    • 0028957841 scopus 로고
    • In vitro assembly of the core catalytic complex of the chloroplast ATP synthase
    • Gao F, Lipscomb B, Wu I and Richter M (1995) In vitro assembly of the core catalytic complex of the chloroplast ATP synthase. J Biol Chem 270: 9763-9769
    • (1995) J Biol Chem , vol.270 , pp. 9763-9769
    • Gao, F.1    Lipscomb, B.2    Wu, I.3    Richter, M.4
  • 35
    • 0343223560 scopus 로고
    • Effect of the interaction between cation-ATP complexes and free cations on ATPase activity in Chromatium strain D chromatophores
    • September 2-6, Elsevier, Amsterdam, The Netherlands
    • Gepshstein A, Hochman Y and Carmeli C (1974) Effect of the interaction between cation-ATP complexes and free cations on ATPase activity in Chromatium strain D chromatophores. In: Proceedings of the Third International Congress on Photosynthesis, September 2-6, pp 1189-1197. Elsevier, Amsterdam, The Netherlands,
    • (1974) Proceedings of the Third International Congress on Photosynthesis , pp. 1189-1197
    • Gepshstein, A.1    Hochman, Y.2    Carmeli, C.3
  • 36
    • 0024288936 scopus 로고
    • Characterization of six nucleotide-binding sites on chloroplast coupling Factor 1 and one site on its purified β subunit
    • Girault G, Berger G, Galmiche J-M and André F (1988) Characterization of six nucleotide-binding sites on chloroplast coupling Factor 1 and one site on its purified β subunit. J Biol Chem 263: 14690-14695
    • (1988) J Biol Chem , vol.263 , pp. 14690-14695
    • Girault, G.1    Berger, G.2    Galmiche, J.-M.3    André, F.4
  • 37
    • 0025661959 scopus 로고
    • Ligand-dependent structural variations in Escherichia coli F1-ATPase revealed by cryoelectron microscopy
    • Gogol E, Johnston E, Aggeler R and Capaldi R (1990) Ligand-dependent structural variations in Escherichia coli F1-ATPase revealed by cryoelectron microscopy. Proc Natl Acad Sci USA 88: 9585-9589
    • (1990) Proc Natl Acad Sci USA , vol.88 , pp. 9585-9589
    • Gogol, E.1    Johnston, E.2    Aggeler, R.3    Capaldi, R.4
  • 38
    • 0020491305 scopus 로고
    • Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase
    • Gresser M, Myers J and Boyer P (1982) Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. J Biol Chem 257: 12030-12038
    • (1982) J Biol Chem , vol.257 , pp. 12030-12038
    • Gresser, M.1    Myers, J.2    Boyer, P.3
  • 39
    • 0000217617 scopus 로고
    • Characterization of two nucleotide binding sites on the isolated, reconstitutively active β subunit of the F0-F1 ATP synthase
    • Gromet-Elhanan Z and Khananshvili D (1984) Characterization of two nucleotide binding sites on the isolated, reconstitutively active β subunit of the F0-F1 ATP synthase. Biochemistry 23: 1022-1028
    • (1984) Biochemistry , vol.23 , pp. 1022-1028
    • Gromet-Elhanan, Z.1    Khananshvili, D.2
  • 40
    • 0020491269 scopus 로고
    • Mechanism of ATP hydrolysis by beef heart mitochondrial F1-ATPase. Rate constants for elementary steps in catalysis at a single site
    • Grubmeyer C, Cross R and Penefsky H (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial F1-ATPase. Rate constants for elementary steps in catalysis at a single site. J Biol Chem 257: 12092-12100
    • (1982) J Biol Chem , vol.257 , pp. 12092-12100
    • Grubmeyer, C.1    Cross, R.2    Penefsky, H.3
  • 42
    • 0027507106 scopus 로고
    • The 'non-exchangeable' nucleotides of F1-F0ATP synthase Cofactors in hydrolysis?
    • Harris D (1993) The 'non-exchangeable' nucleotides of F1-F0ATP synthase Cofactors in hydrolysis? FEBS Lett 316: 209-215
    • (1993) FEBS Lett , vol.316 , pp. 209-215
    • Harris, D.1
  • 43
    • 0029915379 scopus 로고    scopus 로고
    • Structural stability of chloroplast coupling factor 1 as determined by differential scanning calorimetry and cold inactivation
    • Hightower K and Me Carty R (1996a) Structural stability of chloroplast coupling factor 1 as determined by differential scanning calorimetry and cold inactivation. Biochemistry 35: 4852-4857
    • (1996) Biochemistry , vol.35 , pp. 4852-4857
    • Hightower, K.1    Me Carty, R.2
  • 44
    • 0029757152 scopus 로고    scopus 로고
    • Influence of nucleotides on the cold stability of chloroplast coupling factor 1
    • Hightower K and Me Carty R (1996b) Influence of nucleotides on the cold stability of chloroplast coupling factor 1. Biochemistry 35: 10051-10057
    • (1996) Biochemistry , vol.35 , pp. 10051-10057
    • Hightower, K.1    Me Carty, R.2
  • 46
    • 0028280486 scopus 로고
    • Asymmetry of the three catalytic sites on β subunits of TF1 from a thermophilic Bacillus strain PS3
    • Hisabori T, Kobayashi H, Kaibara C and Yoshida M (1994) Asymmetry of the three catalytic sites on β subunits of TF1 from a thermophilic Bacillus strain PS3. J Biochem 115: 497-501
    • (1994) J Biochem , vol.115 , pp. 497-501
    • Hisabori, T.1    Kobayashi, H.2    Kaibara, C.3    Yoshida, M.4
  • 47
    • 0022786781 scopus 로고
    • ADP binding to TF1 and its subunits induces ultraviolet spectral changes
    • Hisabori T, Yoshida M and Sakurai H (1986) ADP binding to TF1 and its subunits induces ultraviolet spectral changes. Biochemistry 100: 663-670
    • (1986) Biochemistry , vol.100 , pp. 663-670
    • Hisabori, T.1    Yoshida, M.2    Sakurai, H.3
  • 48
    • 0017228995 scopus 로고
    • Relations between divalent cation binding and ATPase activity in coupling factor from chloroplast
    • Hochman Y, Lanir A and Carmeli C (1976) Relations between divalent cation binding and ATPase activity in coupling factor from chloroplast. FEBS Lett 61: 255-259
    • (1976) FEBS Lett , vol.61 , pp. 255-259
    • Hochman, Y.1    Lanir, A.2    Carmeli, C.3
  • 50
    • 0028049485 scopus 로고
    • Coordination of nucleotides to metals at the M2 and M3 metal-binding sites of spinach chloroplast F1-ATPase
    • Houseman A, LoBrutto R and Frasch W (1994a) Coordination of nucleotides to metals at the M2 and M3 metal-binding sites of spinach chloroplast F1-ATPase. Biochemistry 33: 10000-10006
    • (1994) Biochemistry , vol.33 , pp. 10000-10006
    • Houseman, A.1    LoBrutto, R.2    Frasch, W.3
  • 52
    • 0028908179 scopus 로고
    • Effects of nucleotides on the protein ligands to metals at the M2 and M3 metal-binding sites of the spinach chloroplast Fl-ATPase
    • Houseman L, LoBrutto R and Frasch W (1995) Effects of nucleotides on the protein ligands to metals at the M2 and M3 metal-binding sites of the spinach chloroplast Fl-ATPase. Biochemistry 34: 3277-3285
    • (1995) Biochemistry , vol.34 , pp. 3277-3285
    • Houseman, L.1    LoBrutto, R.2    Frasch, W.3
  • 53
    • 0027532547 scopus 로고
    • Inhibition by tentoxin of cooperativity among nucleotide binding sites on chloroplast coupling factor 1
    • Hu N, Mills D, Huchzermeyer B and Richter M (1993) Inhibition by tentoxin of cooperativity among nucleotide binding sites on chloroplast coupling factor 1. J Biol Chem 268: 8536-8540
    • (1993) J Biol Chem , vol.268 , pp. 8536-8540
    • Hu, N.1    Mills, D.2    Huchzermeyer, B.3    Richter, M.4
  • 54
    • 0031052032 scopus 로고    scopus 로고
    • Catalytic properties and sensitivity to tentoxin of Chlamydomonas reinhardtii ATP synthase changed in codon 83 of atpB by site-directed mutagenesis
    • Hu D, Fiedler H, Golan T, Edelan M, Strotmann H, Shavit N and Leu S (1997) Catalytic properties and sensitivity to tentoxin of Chlamydomonas reinhardtii ATP synthase changed in codon 83 of atpB by site-directed mutagenesis. J Biol Chem 272: 5457-5463
    • (1997) J Biol Chem , vol.272 , pp. 5457-5463
    • Hu, D.1    Fiedler, H.2    Golan, T.3    Edelan, M.4    Strotmann, H.5    Shavit, N.6    Leu, S.7
  • 55
    • 50549168907 scopus 로고
    • Measurement of protein-binding phenomena by gel filtration
    • Hummel J and Dreyer W (1962) Measurement of protein-binding phenomena by gel filtration. Biochim Biophys Acta 63: 530-532
    • (1962) Biochim Biophys Acta , vol.63 , pp. 530-532
    • Hummel, J.1    Dreyer, W.2
  • 56
    • 0018801483 scopus 로고
    • Subunit interaction during catalysis
    • Hutton R and Boyer P (1979) Subunit interaction during catalysis. J Biol Chem 254: 9990-9993
    • (1979) J Biol Chem , vol.254 , pp. 9990-9993
    • Hutton, R.1    Boyer, P.2
  • 57
    • 0027982788 scopus 로고
    • Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP
    • Jault J-M and Allison W (1994) Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP. J Biol Chem 269: 319-325
    • (1994) J Biol Chem , vol.269 , pp. 319-325
    • Jault, J.-M.1    Allison, W.2
  • 59
    • 0012141973 scopus 로고
    • Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated β subunit of the F0-F1 ATP synthase is a catalytic site
    • Khananshvili D and Gromet-Elhanan Z (1985) Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated β subunit of the F0-F1 ATP synthase is a catalytic site. Proc Natl Acad Sci USA 82: 1886-1890
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1886-1890
    • Khananshvili, D.1    Gromet-Elhanan, Z.2
  • 60
    • 0027399725 scopus 로고
    • ATP-hydrolysis in chloroplasts: Evidence for the participation of three binding sites
    • Labahn A and Gräber P (1993) ATP-hydrolysis in chloroplasts: Evidence for the participation of three binding sites. Biochim Biophys Acta 1141: 288-296
    • (1993) Biochim Biophys Acta , vol.1141 , pp. 288-296
    • Labahn, A.1    Gräber, P.2
  • 61
    • 84985275163 scopus 로고
    • Dihydrotentoxin: A precursor of tentoxin or its degradation product
    • Liebermann B and Ihu W (1988) Dihydrotentoxin: A precursor of tentoxin or its degradation product. J Basic Microbiol 28: 63-70
    • (1988) J Basic Microbiol , vol.28 , pp. 63-70
    • Liebermann, B.1    Ihu, W.2
  • 62
    • 0028343653 scopus 로고
    • Examination of catalytic activity of the β subunit isolated from chloroplast coupling factor 1
    • Malyan A, Girault G and Berger G (1994) Examination of catalytic activity of the β subunit isolated from chloroplast coupling factor 1. Biochim Biophys Acta 1184: 202-206
    • (1994) Biochim Biophys Acta , vol.1184 , pp. 202-206
    • Malyan, A.1    Girault, G.2    Berger, G.3
  • 64
    • 0029059168 scopus 로고
    • ADP binding induces long-distance structural changes in the β polypeptide of the chloroplast ATP synthase
    • Mills D, Seibold S, Squier T and Richter M (1995) ADP binding induces long-distance structural changes in the β polypeptide of the chloroplast ATP synthase. Biochemistry 34: 6100-6108
    • (1995) Biochemistry , vol.34 , pp. 6100-6108
    • Mills, D.1    Seibold, S.2    Squier, T.3    Richter, M.4
  • 65
    • 84886637975 scopus 로고
    • Interaction of adenine nucleotides with the coupling factor of spinach chloroplasts
    • Nabedryk-Viala E, Calvet P, Thiéry J, Galmiche J-M and Girault G (1977) Interaction of adenine nucleotides with the coupling factor of spinach chloroplasts. FEBS Lett 79: 139-143
    • (1977) FEBS Lett , vol.79 , pp. 139-143
    • Nabedryk-Viala, E.1    Calvet, P.2    Thiéry, J.3    Galmiche, J.-M.4    Girault, G.5
  • 66
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H, Yasuda R, Yoshida M and Kinosita 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, K.4
  • 67
    • 0021759661 scopus 로고
    • Specific binding of coupling factor 1 lacking the δ and ε subunits to thylakoids
    • Patrie W and Me Carty R (1984) Specific binding of coupling factor 1 lacking the δ and ε subunits to thylakoids J Biol Chem 259: 11121-11128
    • (1984) J Biol Chem , vol.259 , pp. 11121-11128
    • Patrie, W.1    Me Carty, R.2
  • 69
    • 0011920870 scopus 로고
    • Synergistic activation of an Mg-specific ATPase activity in chloroplast coupling factor by octylglucoside and tentoxin
    • Pick U, Conrad P, Durbin R and Selman B (1982) Synergistic activation of an Mg-specific ATPase activity in chloroplast coupling factor by octylglucoside and tentoxin. Biochim Biophys Acta 682: 55-58
    • (1982) Biochim Biophys Acta , vol.682 , pp. 55-58
    • Pick, U.1    Conrad, P.2    Durbin, R.3    Selman, B.4
  • 71
    • 0030597047 scopus 로고    scopus 로고
    • Tentoxin has at least two binding sites on CF1 and CF1-ε ATPases isolated from spinach chloroplast
    • Pinet E, Gomis J-M, Girault G, Cavelier F, Verducci J, Noël J-P and André F (1996) Tentoxin has at least two binding sites on CF1 and CF1-ε ATPases isolated from spinach chloroplast. FEBS Lett 395: 217-220
    • (1996) FEBS Lett , vol.395 , pp. 217-220
    • Pinet, E.1    Gomis, J.-M.2    Girault, G.3    Cavelier, F.4    Verducci, J.5    Noël, J.-P.6    André, F.7
  • 73
    • 0029666434 scopus 로고    scopus 로고
    • The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B
    • Raaij M, Abrahams J, Leslie A and Walker J (1996) The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B. Proc Natl Acad Sci USA 93: 6913-6917
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6913-6917
    • Raaij, M.1    Abrahams, J.2    Leslie, A.3    Walker, J.4
  • 74
    • 0030464057 scopus 로고    scopus 로고
    • ATP synthase conditions under which all catalytic sites of the Fl moiety are kinetically equivalent in hydrolyzing ATP
    • Reynafarje B and Pedersen P (1996) ATP synthase conditions under which all catalytic sites of the Fl moiety are kinetically equivalent in hydrolyzing ATP. J Biol Chem 271: 32546-32550
    • (1996) J Biol Chem , vol.271 , pp. 32546-32550
    • Reynafarje, B.1    Pedersen, P.2
  • 75
    • 0028982265 scopus 로고
    • ATP synthesis by the F0F1-ATPase from the thermophilic Bacillus PS3 coreconstituted with bacteriorhodopsin into liposomes
    • Richard P, Pitard B and Rigaud J-L (1995) ATP synthesis by the F0F1-ATPase from the thermophilic Bacillus PS3 coreconstituted with bacteriorhodopsin into liposomes. J Biol Chem 270: 21571-21578
    • (1995) J Biol Chem , vol.270 , pp. 21571-21578
    • Richard, P.1    Pitard, B.2    Rigaud, J.-L.3
  • 76
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F1-ATPase
    • Sabbert D, Engelbrecht S and Junge W (1996) Intersubunit rotation in active F1-ATPase. Nature, 381: 623-625
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 78
    • 0020775079 scopus 로고
    • 1-ATPase in the presence of dimethylsulfoxide
    • 1-ATPase in the presence of dimethylsulfoxide. J Biochem 93, 1601-1614
    • (1983) J Biochem , vol.93 , pp. 1601-1614
    • Sakamoto, J.1    Tonomura, Y.2
  • 79
    • 0028815161 scopus 로고
    • 3 complex of ATP synthase from the thermophilic Bacterium PS3: Structural characteristics shown by time-resolved small-angle X-ray scattering with synchrotron radiation
    • 3 complex of ATP synthase from the thermophilic Bacterium PS3: Structural characteristics shown by time-resolved small-angle X-ray scattering with synchrotron radiation. J Biochem 117: 113-119
    • (1995) J Biochem , vol.117 , pp. 113-119
    • Sato, M.1    Ito, Y.2    Harada, M.3    Kihara, H.4    Tsurata, H.5    Ota, S.6    Kagawa, Y.7
  • 80
    • 0025856007 scopus 로고
    • Four tight nucleotide binding sites of chloroplast coupling factor 1
    • Shapiro A, Huber A and Me Carty R (1991) Four tight nucleotide binding sites of chloroplast coupling factor 1. J Biol Chem 266: 4194-4200
    • (1991) J Biol Chem , vol.266 , pp. 4194-4200
    • Shapiro, A.1    Huber, A.2    Me Carty, R.3
  • 81
    • 0030045540 scopus 로고    scopus 로고
    • 3 core complex: Structure, stability, and catalytic properties
    • 3 core complex: Structure, stability, and catalytic properties. Biochemistry 35: 1242-1248
    • (1996) Biochemistry , vol.35 , pp. 1242-1248
    • Sokolov, M.1    Gromet-Elhanan, Z.2
  • 82
    • 0028124933 scopus 로고
    • Alkylation of cysteine 89 of the y subunit of chloroplast coupling factor 1 with N-ethylmaleimide alters nucleotide interactions
    • Soteropoulos P, Ong A and Me Carty R (1994) Alkylation of cysteine 89 of the y subunit of chloroplast coupling factor 1 with N-ethylmaleimide alters nucleotide interactions. J Biol Chem 269: 19810-19816
    • (1994) J Biol Chem , vol.269 , pp. 19810-19816
    • Soteropoulos, P.1    Ong, A.2    Me Carty, R.3
  • 84
    • 0018265712 scopus 로고
    • Tentoxin, an uncompetitive inhibitor of lettuce chloroplast coupling factor 1
    • Steele J, Durbin R, Uchytil T and Rich D (1978a) Tentoxin, an uncompetitive inhibitor of lettuce chloroplast coupling factor 1. Biochim Biophys Acta 501: 72-82
    • (1978) Biochim Biophys Acta , vol.501 , pp. 72-82
    • Steele, J.1    Durbin, R.2    Uchytil, T.3    Rich, D.4
  • 85
    • 0018082612 scopus 로고
    • The stimulation of coupling factor 1 ATPase by tentoxin
    • Steele J, Uchytil T and Durbin R (1978b) The stimulation of coupling factor 1 ATPase by tentoxin. Biochim Biophys Acta 504: 136-141
    • (1978) Biochim Biophys Acta , vol.504 , pp. 136-141
    • Steele, J.1    Uchytil, T.2    Durbin, R.3
  • 87
    • 0028033832 scopus 로고
    • ATP binding causes a conformational change in the y subunit of the Escherichia cou F1 ATPase which is reversed on bond cleavage
    • Turina P and Capaldi R (1994) ATP binding causes a conformational change in the y subunit of the Escherichia cou F1 ATPase which is reversed on bond cleavage. Biochemistry 33: 14275-14280
    • (1994) Biochemistry , vol.33 , pp. 14275-14280
    • Turina, P.1    Capaldi, R.2
  • 89
    • 33646288211 scopus 로고
    • Hydrogen exchange into soluble spinach chloroplast coupling factor during heat activation of its ATPase
    • Viale A, Vallejos R and Jagendorf A (1981) Hydrogen exchange into soluble spinach chloroplast coupling factor during heat activation of its ATPase. Biochim Biophys Acta 637: 496-503
    • (1981) Biochim Biophys Acta , vol.637 , pp. 496-503
    • Viale, A.1    Vallejos, R.2    Jagendorf, A.3
  • 90
    • 0027384957 scopus 로고
    • Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase
    • Wang Z-Y, Freire E and Me Carty R (1993) Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase. J Biol Chem 268: 20785-20790
    • (1993) J Biol Chem , vol.268 , pp. 20785-20790
    • Wang, Z.-Y.1    Freire, E.2    Me Carty, R.3
  • 91
    • 0028279783 scopus 로고
    • Tryptophan fluorescence provides a direct probe of nucleotide binding in the noncatalytic sites of Escherichia coli F1-ATPase
    • Weber J, Wilke-Mounts S, Grell E and Senior A (1994) Tryptophan fluorescence provides a direct probe of nucleotide binding in the noncatalytic sites of Escherichia coli F1-ATPase. J Biol Chem 269: 11261-11268
    • (1994) J Biol Chem , vol.269 , pp. 11261-11268
    • Weber, J.1    Wilke-Mounts, S.2    Grell, E.3    Senior, A.4
  • 92
    • 0028982275 scopus 로고
    • α-Aspartate 261 is a key residue in noncatalytic sites of Escherichia coli F1-ATPase
    • Weber J, Bowman C, Wilke-Mounts S, Grell E and Senior A (1995) α-Aspartate 261 is a key residue in noncatalytic sites of Escherichia coli F1-ATPase. J Biol Chem 270: 21045-21049
    • (1995) J Biol Chem , vol.270 , pp. 21045-21049
    • Weber, J.1    Bowman, C.2    Wilke-Mounts, S.3    Grell, E.4    Senior, A.5
  • 93
    • 0027946356 scopus 로고
    • Tight nucleotide binding sites and ATPase activities of the Rhodospirillum rubrum RrF1-ATPase as compared to spinach chloroplast CF1-ATPase
    • Weiss S, Me Carty R and Gromet-Elhanan Z (1994) Tight nucleotide binding sites and ATPase activities of the Rhodospirillum rubrum RrF1-ATPase as compared to spinach chloroplast CF1-ATPase. J Bioenerg Biomembr 26: 573-581
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 573-581
    • Weiss, S.1    Me Carty, R.2    Gromet-Elhanan, Z.3
  • 94
    • 0023642550 scopus 로고
    • Catalytic and noncatalytic nucleotide binding sites of Escherichia coli F1-ATPase
    • Wise J, Hicke B and Boyer P (1987) Catalytic and noncatalytic nucleotide binding sites of Escherichia coli F1-ATPase. FEBS Lett 223: 395-401
    • (1987) FEBS Lett , vol.223 , pp. 395-401
    • Wise, J.1    Hicke, B.2    Boyer, P.3
  • 95
    • 0021759019 scopus 로고
    • Kinetics of ATP hydrolysis by F1-ATPase and the effects of anion activation, removal of tightly bound nucleotides, and partial inhibition of the ATPase by covalent modification
    • Wong S, Matsuno-Yagi A and Hatefi Y (1984) Kinetics of ATP hydrolysis by F1-ATPase and the effects of anion activation, removal of tightly bound nucleotides, and partial inhibition of the ATPase by covalent modification. Biochemistry 23: 5004-5009
    • (1984) Biochemistry , vol.23 , pp. 5004-5009
    • Wong, S.1    Matsuno-Yagi, A.2    Hatefi, Y.3
  • 96
    • 0023642574 scopus 로고
    • Catalytic and Non catalytic sites nucleotide binding sites of chloroplast F1 ATPase
    • Xue Z, Miller C, Zhou J-M and Boyer P (1987) Catalytic and Non catalytic sites nucleotide binding sites of chloroplast F1 ATPase. FEBS Lett 223: 391-394
    • (1987) FEBS Lett , vol.223 , pp. 391-394
    • Xue, Z.1    Miller, C.2    Zhou, J.-M.3    Boyer, P.4
  • 97
    • 0022975890 scopus 로고
    • Characterization of the catalytic and noncatalytic ADP binding sites of the F1-ATPase from the thermophilic Bacterium, PS3
    • Yoshida M and Allison W (1986) Characterization of the catalytic and noncatalytic ADP binding sites of the F1-ATPase from the thermophilic Bacterium, PS3. J Biol Chem 261: 5714-5721
    • (1986) J Biol Chem , vol.261 , pp. 5714-5721
    • Yoshida, M.1    Allison, W.2
  • 98
    • 0028967017 scopus 로고
    • Some unique characteristics of thylakoid unisite ATPase
    • Zhang S and Jagendorf A (1995) Some unique characteristics of thylakoid unisite ATPase. J Biol Chem 270: 6607-6614
    • (1995) J Biol Chem , vol.270 , pp. 6607-6614
    • Zhang, S.1    Jagendorf, A.2
  • 99
    • 0026611758 scopus 로고
    • 2+ requirement for photophosphorylation
    • 2+ requirement for photophosphorylation. Biochemistry 31: 3166-3171
    • (1992) Biochemistry , vol.31 , pp. 3166-3171
    • Zhou, J.1    Boyer, P.2
  • 100
    • 0030592156 scopus 로고    scopus 로고
    • ATP hydrolysis by membrane-bound Escherichia coli FOF1 causes rotation of the γ subunit relative to the β subunits
    • Zhou Y Duncan T, Bulygin V, Hutcheon M and Cross R (1996) ATP hydrolysis by membrane-bound Escherichia coli FOF1 causes rotation of the γ subunit relative to the β subunits. Biochim Biophys Acta 1275: 96-100
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 96-100
    • Zhou, Y.1    Duncan, T.2    Bulygin, V.3    Hutcheon, M.4    Cross, R.5


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