The Relationship Between the Structure and Catalytic Mechanism of the Chloroplast ATP Synthase

  • Mark L. Richter
  • Denise A. Mills
Part of the Advances in Photosynthesis and Respiration book series (AIPH, volume 4)


An overview of the nucleotide binding properties and current models of the catalytic mechanism of the chloroplast ATP synthase is presented. The discussion includes consideration of the role of the small subunits of the catalytic chloroplast coupling factor 1 (CF1) in gating the flow of protons across the membrane. Some emphasis is placed on the potential role of the ε subunit in a proton-driven activation process and an apparent role of this subunit in influencing cooperativity among the different nucleotide binding sites on both membrane-bound and isolated CF1 Controversy over the type of nucleotide binding sites on CF1 is discussed, together with the potential involvement of the different nucleotide binding sites in the catalytic process.


Nucleotide Binding Coupling Factor Nucleotide Binding Site Spinach Chloroplast Rhodospirillum Rubrum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abrahams JP, Lutter R, Todd RJ, van Raaij MJ, Leslie AGW and Walker JE (1993) Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5Å resolution. EMBO J 12: 1775–1780PubMedGoogle Scholar
  2. Abrahams JP, Leslie AGW, Lutter R and Walker JE (1994) Structure at 2.8Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621–628PubMedCrossRefGoogle Scholar
  3. Admon A and Hammes GG (1987) Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1. Biochemistry 26: 3193–3197PubMedCrossRefGoogle Scholar
  4. Aflalo C and Shavit N (1982) Source of rapidly labeled ATP tightly bound to non-catalytic sites on the chloroplast ATP synthase. Eur J Biochem 126: 61–68PubMedCrossRefGoogle Scholar
  5. Andralojc PJ and Harris DA (1992) Isolation and characterization of a functional αβ heterodimer from ATP synthase of Rhodospirillum rubrum. FEBS Lett 310: 187–192PubMedCrossRefGoogle Scholar
  6. Anthon GE and Jagendorf AT (1986) Evidence for multiple effects in methanol activation of chloroplast coupling factor 1. Biochim Biophys Acta 848: 92–98PubMedGoogle Scholar
  7. Avital S and Gromet-Elhanan Z (1991) Extraction and purification of the beta subunit and an active alpha-beta-core complex from the spinach chloroplast CF0F1 ATP synthase. J Biol Chem 266: 7067–7072PubMedGoogle Scholar
  8. Avron M and Jagendorf AT (1959) Evidence concerning the mechanism of adenine triphosphate formation by spinach chloroplasts. J Biol Chem 234: 967–972PubMedGoogle Scholar
  9. Bakker-Grunwald T and van Dam K (1974) On the mechanism of activation of the ATPase in chloroplasts. Biochim Biophys Acta 347: 290–298PubMedGoogle Scholar
  10. Bar-Zvi D and Shavit N (1980) Role of the tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities. FEBS Lett 119: 68–72CrossRefGoogle Scholar
  11. Bar-Zvi D and Shavit N (1982) Modulation of the chloroplast ATPase by tight ADP binding: Effect of uncouplers and ATP. J Bioenerg Biomemb 14: 467–478Google Scholar
  12. Bar-Zvi D, Teifert MA and Shavit N (1983) Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-0-(4-benzoyl)benzoyl adenosine 5′-diphosphate. FEBS Lett 160: 233–238CrossRefGoogle Scholar
  13. Beckers G, Berzborn RJ and Strotmann H (1992) Zero-length cross-linking between subunits δ and I of the H+-translocating ATPase of chloroplasts. Biochim Biophys Acta 1101: 97–104PubMedGoogle Scholar
  14. Beharry S and Bragg PD (1992) E. coli F1-ATPase can use GTP-nonchaseable bound adenine nucleotide to synthesize ATP in DMSO. Biochemistry 31: 11472–11476PubMedCrossRefGoogle Scholar
  15. Berden JA, Hartog AF and Edel CM (1991) Hydrolysis of ATP can be described only on the basis of a dual-site mechanism. Biochim Biophys Acta 1057: 151–156PubMedGoogle Scholar
  16. Berg HC (1975) Bacterial behavior. Nature 254: 389–392PubMedCrossRefGoogle Scholar
  17. Bianchet M, Xavier Y, Hullihen J, Pedersen PL and Amzel M (1991) Mitochondrial ATP synthase: Quaternary structure of the F1 moiety at 3.6Å determined by X-ray diffraction analysis. J Biol Chem 266: 21197–21201PubMedGoogle Scholar
  18. Bickel-Sandkötter S and Strotmann H (1981) Nucleotide binding and regulation of chloroplast ATP synthase. FEBS Lett 125: 188–192Google Scholar
  19. Boyer PD (1987) The unusual enzymology of ATP synthase. Biochemistry 26: 8503–8507PubMedCrossRefGoogle Scholar
  20. Boyer PD (1993) The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim Biophys Acta 1140: 215–250PubMedGoogle Scholar
  21. Boyer PD and Kohlbrenner WE (1981) The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts. In: R Selman and Selman-Reimer S (eds) Energy Coupling in Photosynthesis pp 230–240. Elsevier, AmsterdamGoogle Scholar
  22. Boynton JE, Gilham NW, Harris JP, Johnson AM, Jones AR, Randalf-Anderson BL, Robertson D, Klein TM, Shark KB and Sanford JC (1988) Chloroplast transformation in Chlamydomonas with high velocity projectiles. Science 240: 1534–1538PubMedGoogle Scholar
  23. Bruist MF and Hammes GG (1981) Further characterization of nucleotide binding sites on chloroplast coupling factor one. Biochemistry 20: 6298–6305PubMedCrossRefGoogle Scholar
  24. Bruist MF and Hammes GG (1982) Mechanism for catalysis and regulation of adenosine 5′-triphosphate hydrolysis by chloroplast coupling factor. Biochemistry 21: 3370–3377PubMedCrossRefGoogle Scholar
  25. Carlier MF and Hammes GG (1979) Interaction of nucleotides with chloroplast coupling factor 1. Biochemistry 18: 3446–3451PubMedGoogle Scholar
  26. Cerione RA and Hammes GG (1982) Structural mapping of nucleotide binding sites on chloroplast coupling factor. Biochemistry 21: 745–752PubMedCrossRefGoogle Scholar
  27. Chaney SG and Boyer PD (1969) Lack of detection of intermediates in the path of phosphorylative oxidation to water in photophosphorylation. J Biol Chem 244: 5773–5778PubMedGoogle Scholar
  28. Chen GG and Jagendorf AT (1994) Chloroplast molecular chaperone-assisted refolding and reconstitution of an active multi-subunit CF1 core. Proc Natl Acad Sci USA: 11497–11501Google Scholar
  29. Chen Z, Wu I and Richter ML (1992) Over-expression and refolding of β-subunit from chloroplast ATP synthase. FEBS Lett 298: 69–73PubMedCrossRefGoogle Scholar
  30. Colvert KC, Mills DA and Richter ML (1992) Structural mapping of cysteine-63 of the chloroplast ATP synthase β subunit. Biochemistry 31: 3930–3935PubMedCrossRefGoogle Scholar
  31. Cox GB, Jans DA, Fimmel AL, Gibson F and Hatch L (1984) The mechanism of ATP synthase: Conformational change by rotation of the β-subunit. Biochim Biophys Acta 768: 201–208PubMedGoogle Scholar
  32. Cross RL (1981) The mechanism and regulation of ATP synthesis by F1-ATPases. Ann Rev Biochem 50: 681–714PubMedGoogle Scholar
  33. Cross RL (1988) The number of functional sites on F1-ATPases and the effects of quaternary structural asymmetry on their properties. J Bioenerg Biomemb 20: 395–406Google Scholar
  34. Cross RL (1992). The reaction mechanism of F0F1-ATPsynthases. In: Ernster L (ed) Molecular Mechanisms in Bioenergetics pp 317–330. Elsevier, AmsterdamGoogle Scholar
  35. Cross RL and Nalin CM (1982) Adenine nucleotide binding sites on beef-heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three non-catalytic sites. J Biol Chem 257: 2874–2881PubMedGoogle Scholar
  36. Cross RL, Cunningham D, Miller CG, Xue Z, Zhou J-M and Boyer PD (1987) Adenine nucleotide binding sites on beef heart F1 ATPase: Photoaffinity labeling of β subunit Tyr 368 at a non-catalytic site and Tyr 345 at a catalytic site. Proc Natl Acad Sci USA 84: 5715–5719PubMedGoogle Scholar
  37. Devlin CC and Grisham CM (1990) 1H and 31P Nuclear magnetic resonance and kinetic studies of the active site structure of chloroplast CF1 ATP synthase. Biochemistry 29: 6192–6203PubMedCrossRefGoogle Scholar
  38. Duncan TM and Cross RL (1992) A model for the catalytic site of F1-ATPase based on analogies to nucleotide-binding domains of known structure. J Bioenerg Biomemb 24: 453–461Google Scholar
  39. Duncan TM and Senior AE (1985) The defective proton-ATPase of uncD mutants of Escherichia coli: Two mutations which affect the catalytic mechanism. J Biol Chem 260: 4901–4907PubMedGoogle Scholar
  40. Engelbrecht S and Junge W (1988) Purified subunit δ of chloroplast coupling factor CF1 reconstitutes photophosphorylation in partially-CF1 depleted membranes. Eur J Biochem 172: 213–218PubMedCrossRefGoogle Scholar
  41. Fromme P and Gräber P (1990a) Activation/inactivation and unisite catalysis by the reconstituted ATP-synthase from chloroplasts. Biochim Biophys Acta 1016: 29–42PubMedGoogle Scholar
  42. Fromme P and Gräber P (1990b) ATP-hydrolysis in chloroplasts: Uni-site catalysis and evidence for heterogeneity of sites. Biochim Biophys Acta 1020: 187–194Google Scholar
  43. Gao F, Lipscomb B, Wu I and Richter ML (1995) In vitro assembly of the core catalytic complex of the chloroplast ATP synthase. J Biol Chem 270: 9763–9769PubMedCrossRefGoogle Scholar
  44. Girault G, Berger G, Galmiche J-M and Andre F (1988) Characterization of six nucleotide binding sites of chloroplast coupling factor 1 and one site on its purified β subunit. J Biol Chem 263: 14690–14695PubMedGoogle Scholar
  45. Gogol E, Johnston E, Aggeler R and Capaldi R (1990) Ligand-dependent structural variations in E. coli F1-ATPase revealed by cryoelectron microscopy. Biochemistry 29: 9585–9589Google Scholar
  46. Gräber P, Schlodder E and Witt HT (1977) Conformational change of the chloroplast ATPase induced by a transmembrane electric field and its correlation to phosphorylation. Biochim Biophys Acta 461: 426–440PubMedGoogle Scholar
  47. Gresser MJ, Meyers JA and Boyer PD (1982) Catalytic site cooperativity of beef heart mitochondrial F1-ATPase. J Biol Chem 257: 12030–12038PubMedGoogle Scholar
  48. Gromet-Elhanan Z (1992) Identification of the subunits required for the catalytic activity of the F1-ATPase. J Bioenerg Biomemb 24: 447–452Google Scholar
  49. Gromet-Elhanan Z and Avital S (1992) Properties of the catalytic (αβ)-core complex of chloroplast CF1-ATPase. Biochim Biophys Acta 1102: 379–385Google Scholar
  50. Gromet-Elhanan Z and Khanashvili D (1984) Characterization of two nucleotide binding sites on the isolated, reconstitutively active β subunit of the F0F1 ATP synthase. Biochemistry 23: 1022–1028CrossRefGoogle Scholar
  51. Grubmeyer C, Cross RL and Penefsky HS (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. J Biol Chem 257: 12092–12100PubMedGoogle Scholar
  52. Guerrero KJ, Ehler LL and Boyer PD (1990) Guanosine and formycin triphosphates bind at non-catalytic nucleotide binding sites of CF1 ATPase and inhibit ATP hydrolysis. FEBS Lett 270: 187–190PubMedCrossRefGoogle Scholar
  53. Hackney DD and Boyer PD (1978) Subunit interaction during catalysis: Implications of concentration dependency of oxygen exchange accompanying oxidative phosphorylation for alternating site cooperativity. J Biol Chem 253: 3164–3170PubMedGoogle Scholar
  54. Hackney DD, Rosen G and Boyer PD (1979) Subunit interaction during catalysis. Alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O] ATP species formation. Proc Natl Acad Sci USA 76: 3646–3650PubMedGoogle Scholar
  55. Haddy AE and Sharp RR (1989) Field dependence of solvent proton and deuteron NMR relaxation rates of the manganese (II) binding site of chloroplast coupling factor 1. Biochemistry 28: 3656–3664Google Scholar
  56. Harris DA (1993) The ‘non-exchangeable’ nucleotides of F1-F0 ATP synthase; Cofactors in hydrolysis? FEBS Lett 316: 209–215PubMedCrossRefGoogle Scholar
  57. Harris DA and Crofts AR (1978) The initial stages of photophosphorylation: Studies using excitation by saturating, short flashes of light. Biochim Biophys Acta 502: 87–102PubMedGoogle Scholar
  58. Harris DA and Slater EC (1975) Tightly-bound nucleotides of the energy-transducing ATPase of chloroplasts and their role in photophosphorylation. Biochim Biophys Acta 387: 335–348PubMedGoogle Scholar
  59. Hiller R and Carmeli C (1985) Cooperativity among manganese-binding sites in the H-ATPase of chloroplasts. J Biol Chem 260: 1614–1617PubMedGoogle Scholar
  60. Hisabori T, Muneyuki E, Odaka M, Yokoyama K, Mochizuki K and Yoshida M (1992) Single site hydrolysis of 2′3′-O-(2,4,6-trinitrophenyl)-ATP by the F1-ATPase from the thermophilic bacterium PS3 is accelerated by the chase-addition of excess ATP. J Biol Chem 267: 4551–4556PubMedGoogle Scholar
  61. Hochman Y and Carmeli C (1981) Correlation between the kinetics of activation and inhibition of adenosine triphosphatase activity by divalent metal ions and the binding of manganese to chloroplast coupling factor 1. Biochemistry 20: 6287–6292PubMedGoogle Scholar
  62. Hochman Y, Lanir A and Carmeli C (1976) Relations between divalent cation binding and ATPase activity in coupling factor from chloroplast. FEBS Lett 61: 255–259PubMedCrossRefGoogle Scholar
  63. Hu N, Mills DA, Huchzermeyer B and Richter ML (1993) Inhibition by tentoxin of cooperativity among nucleotide binding sites on chloroplast coupling factor 1. J Biol Chem 268: 8536–8540PubMedGoogle Scholar
  64. Huchzermeyer B (1988a) Nucleotide binding and ATPase activity of membrane bound chloroplast coupling factor (CF1). Z Naturforsch 43: 133–139Google Scholar
  65. Huchzermeyer B (1988b) Phosphate binding to isolated chloroplast coupling factor (CF1). Z Naturforsch 43: 213–218Google Scholar
  66. Ishii N, Yoshimura H, Nagayama K, Kagawa Y and Yoshida M (1993) Three dimensional structure of F1-ATPase of thermophilic bacterium PS3 obtained by electron crystallography. J Biochem (Tokyo) 113: 245–250Google Scholar
  67. Johnson LN, Acharya KR, Jordan MD and McLaughlin PJ (1990) Refined crystal structure of the phosphorylase-heptulose-2-phosphate-oligosaccharide-AMP complex. J Mol Biol 211: 645–661PubMedCrossRefGoogle Scholar
  68. Kambouris NG and Hammes GG (1985) Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3′-O-(4-benzoyl)benzoyl adenosine 5′-triphosphate. Proc Natl Acad Sci (USA) 82: 1950–1953Google Scholar
  69. Kayalar C, Rosing J and Boyer PD (1977) An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions. J Biol Chem 252: 2486–2491PubMedGoogle Scholar
  70. Khananshvili D and Gromet-Elhanan Z (1982) Isolation and purification of an active γ subunit of the F0F1-ATP synthase from chromatophore membranes of Rhodospirillum rubrum. J Biol Chem 257: 11377–11383PubMedGoogle Scholar
  71. Khananshvili D and Gromet-Elhanan Z (1984) Demonstration of two binding sites for ADP on the isolated β-subunit of the Rhodospirillum rubrum RF0F1-ATP synthase. FEBS Lett 178: 10–14CrossRefGoogle Scholar
  72. Kironde FA and Cross RL (1986) Adenine nucleotide-binding sites on beef heart F1-ATPase: Conditions that affect occupancy of catalytic and non-catalytic sites. J Biol Chem 261: 12544–12549PubMedGoogle Scholar
  73. Kohlbrenner WE and Boyer PD (1983) Probes of catalytic site cooperativity during catalysis by the chloroplast ATPase and the ATP synthase. J Biol Chem 258: 10881–10886PubMedGoogle Scholar
  74. Komatsu-Takaki M (1989) Energy-dependent conformational changes in the epsilon subunit of the chloroplast ATP synthase. J Biol Chem 264: 17750–17753PubMedGoogle Scholar
  75. Larson EM and Jagendorf AT (1986) Anion stimulation of ATPase in activated spinach chloroplast coupling factor 1 (CF1); Light activation mimic? Plant Physiol 80: S251CrossRefGoogle Scholar
  76. Leckband D and Hammes GG (1987) Interactions between nucleotide binding sites on chloroplast coupling factor 1 during ATP hydrolysis. Biochemistry 26: 2306–2312PubMedCrossRefGoogle Scholar
  77. Leckband D and Hammes GG (1988) Function of tightly bound nucleotides on membrane-bound chloroplast coupling factor. Biochemistry 27: 3629–3633PubMedCrossRefGoogle Scholar
  78. Lill H, Burkovski A, Altendorf K, Junge W and Engelbrecht S (1993) Complementation of Escherichia coli unc mutant strains by chloroplast and cyanobacterial F1-ATPase subunits. Biochim Biophys Acta 1144: 278–284PubMedGoogle Scholar
  79. Lohse D, Thelen R and Strotmann H (1989) Activity equilibria of the thiol-modulated chloroplast H+-ATPase as a function of the proton gradient in the absence and presence of ADP and arsenate. Biochim Biophys Acta 976: 85–93Google Scholar
  80. Magnusson RP and McCarty RE (1976) Light-induced exchange of nucleotides into coupling factor 1 in spinach chloroplast thylakoids. J Biol Chem 251: 7417–7422PubMedGoogle Scholar
  81. McCarty RE and Fagan J (1973) Incorporation of N-ethylmaleimide into coupling factor 1 in spinach chloroplasts. Biochemistry 12: 1503–1507PubMedCrossRefGoogle Scholar
  82. Michel L, Garin J, Girault G and Vignais PV (1992) Photolabeling of the phosphate binding site of chloroplast coupling factor 1 with [32P]azidonitrophenyl phosphate. FEBS Lett 313: 90–93PubMedCrossRefGoogle Scholar
  83. Milgrom YM and Murataliev MB (1987) Characterization of the nucleotide tight-binding sites of the isolated mitochondrial F1-ATPase. FEBS Lett 219: 156–160PubMedCrossRefGoogle Scholar
  84. Milgrom YM, Ehler LL and Boyer PD (1990) ATP binding at non-catalytic sites of soluble CF1 is required for expression of the enzyme activity. J Biol Chem 265: 18725–18728PubMedGoogle Scholar
  85. Milgrom YM, Ehler LL and Boyer PD (1991) The characteristics and effect on activity of nucleotide binding to non-catalytic sites of CF1-ATPase. J Biol Chem 266: 11551–11558PubMedGoogle Scholar
  86. Mills DA and Richter ML (1991) Nucleotide binding to the isolated β subunit of the chloroplast ATP synthase. J Biol Chem 266: 7440–7444PubMedGoogle Scholar
  87. Mills DA, Seibold SA, Squier TC and Richter ML (1995) ADP binding induces long-distance structural changes in the β polypeptide of the chloroplast ATP synthase. Biochemistry 34: 6100–6108PubMedCrossRefGoogle Scholar
  88. Moroney JV and McCarty RE (1979) Reversible uncoupling of photophosphorylation by a new bifunctional maleimide. J Biol Chem 254: 8951–8955PubMedGoogle Scholar
  89. Moroney JV and McCarty RE (1982) Light-dependent cleavage of the subunit of coupling factor 1 by trypsin causes activation of Mg2+-ATPase activity and uncoupling of photophosphorylation in spinach chloroplasts. J Biol Chem 257: 5915–5920PubMedGoogle Scholar
  90. Nalin CM and Nelson N (1987) Structure and biogenesis of chloroplast coupling factor CF0CF1-ATPase. Curr Top Bioenerg 15: 273–294Google Scholar
  91. Nalin CM, Snyder B and McCarty RE (1985) Selective modification of an α subunit of chloroplast coupling factor 1. Biochemistry 24: 2318–2324PubMedCrossRefGoogle Scholar
  92. Nelson N, Nelson H and Racker E (1972) Partial resolution of the enzymes catalyzing photophosphorylation: Purification and properties of an inhibitor isolated from chloroplast coupling factor 1. J Biol Chem 247: 7657–7662PubMedGoogle Scholar
  93. Noumi T, Taniai M, Kananzawa H and Futai M (1986) Replacement of arginine 246 by histidine in the β subunit of Escherichia coli H+-ATPase resulted in loss of multi-site ATPase activity. J Biol Chem 261: 9196–9201PubMedGoogle Scholar
  94. Penefsky HS and Cross RL (1991) Structure and mechanism of F0F1-type ATP synthases and ATPases. Advances in Enzymology and Related Areas of Molecular Biology 64: 173–214PubMedGoogle Scholar
  95. Philosoph S, Binder A and Gromet-Elhanan Z (1977) Coupling factor ATPase complex of R. rubrum. J Biol Chem 252: 8747–8752PubMedGoogle Scholar
  96. Richter ML and McCarty RE (1987) Energy-dependent changes in the conformation of the ε subunit of the chloroplast ATP synthase. J Biol Chem 262: 15037–15040PubMedGoogle Scholar
  97. Richter ML, Patrie WJ and McCarty RE (1984) Preparation of the ε subunit and ε subunit-deficient chloroplast coupling factor 1 in reconstitutively active forms. J Biol Chem 259: 7371–7373PubMedGoogle Scholar
  98. Richter ML, Snyder B, McCarty RE and Hammes GG (1985) Binding stoichiometry and structural mapping of the ε polypeptide of chloroplast coupling factor 1. Biochemistry 24: 5755–5763PubMedCrossRefGoogle Scholar
  99. Richter ML, Gromet-Elhanan Z and McCarty RE (1986) Reconstitution of the H+-ATPase complex of Rhodospirillum rubrum by the β subunit of the chloroplast coupling factor 1. J Biol Chem 261: 12109–12113PubMedGoogle Scholar
  100. Rosen G, Gresser M, Vinkler C and Boyer PD (1979) Assessment of total catalytic sites and the nature of bound nucleotide participation in photophosphorylation. J Biol Chem 254: 10654–10661PubMedGoogle Scholar
  101. Rosing J, Smith DJ, Kayalar C and Boyer PD (1976) Medium ADP and not ADP already tightly bound to thylakoid membranes forms the initial ATP in chloroplast phosphorylation. Biochem Biophys Res Commun 72: 1–8PubMedCrossRefGoogle Scholar
  102. Roux-Fromy M, Neumann J-M, Andre F, Berger G, Girault G, Galmiche J-M, and Remy R (1987) Biochemical and proton NMR characterization of the isolated functional beta-subunit of coupling factor one from spinach chloroplasts. Biochem Biophys Res Commun 144: 718–725PubMedGoogle Scholar
  103. Roy H and Moudrianakis EN (1971) Interactions between ADP and the coupling factor of photophosphorylation. Proc Natl Acad Sci USA 68: 2720–2724PubMedGoogle Scholar
  104. Ryrie IJ and Jagendorf AT (1972) Correlation between a conformational change in the coupling factor protein and the high energy state in chloroplasts. J Biol Chem 247: 4453–4459PubMedGoogle Scholar
  105. Schumann J (1981) Adenine nucleotide binding to CF1 and ATPase activity of chloroplasts. In: R Selman and Selman-Reimer S (eds) Energy Coupling in Photosynthesis Research, pp 223–230. Elsevier, North HollandGoogle Scholar
  106. Schumann J (1984) A study on the exchange of tightly bound nucleotides on the membrane-associated chloroplast ATP synthase complex. Biochim Biophys Acta 766: 334–342Google Scholar
  107. Schumann J, Richter ML and McCarty RE (1985) Partial proteolysis as a probe of the conformation of the γ subunit in activated soluble and membrane-bound chloroplast coupling factor. J Biol Chem 260: 11817–11830PubMedGoogle Scholar
  108. Shapiro AB and McCarty RE (1990) Substrate binding-induced alteration of nucleotide binding site properties of chloroplast coupling factor 1. J Biol Chem 265: 4340–4347PubMedGoogle Scholar
  109. Shapiro AB and McCarty RE (1991) Four tight nucleotide binding sites of chloroplast coupling factor 1. J Biol Chem 266: 4194–4200PubMedGoogle Scholar
  110. Shapiro A, Gibson KD, Scheraga H and McCarty RE (1991) Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1. J Biol Chem 266: 17276–17285PubMedGoogle Scholar
  111. Shavit N, Skye GE and Boyer PD (1967) Occurrence and possible mechanism of 32P and 18O exchange reactions of photophosphorylation. J Biol Chem 242: 5125–5130PubMedGoogle Scholar
  112. Sherman PA and Wimmer MJ (1982) Two types of kinetic regulation of the activated ATPase in the chloroplast photophosphorylation system. J Biol Chem 257: 7012–7017PubMedGoogle Scholar
  113. Sherman PA and Wimmer MJ (1983) Kinetic effects of chemical and physical uncoupling on the energy-transducing ATPase from spinach chloroplasts. Eur J Biochem 136: 539–543PubMedCrossRefGoogle Scholar
  114. Shoshan V and Selman BR (1979) The relationship between light-induced adenine nucleotide exchange and ATPase activity in chloroplast thylakoid membranes. J Biol Chem 254: 8801–8807PubMedGoogle Scholar
  115. Snyder B and Hammes GG (1984) Structural mapping of chloroplast coupling factor. Biochemistry 23: 5787–5795PubMedCrossRefGoogle Scholar
  116. Soteropoulos P, Suss K-H and McCarty RE (1992) Modifications of the γ subunit of chloroplast coupling factor 1 alter interactions with the inhibitory ε subunit. J Biol Chem 267: 10348–10354PubMedGoogle Scholar
  117. Spencer JC and Wimmer MJ (1985) Mechanisms by which reactions catalyzed by chloroplast coupling factor 1 are inhibited: ATP synthesis and ATP-H2O oxygen exchange. Biochemistry 24: 3884–3890PubMedCrossRefGoogle Scholar
  118. Stroop SD and Boyer PD (1985) Characteristics ofthe chloroplast ATP synthase as revealed by reaction at low ADP concentrations. Biochemistry 24: 2304–2310CrossRefGoogle Scholar
  119. Strotmann H, Bickel S and Huchzermeyer B (1976) Energy-dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF1. FEBS Lett 61: 194–198PubMedCrossRefGoogle Scholar
  120. Strotmann H, Bickel-Sandkötter S and Shoshan V (1979) Kinetic analysis of light-dependent exchange of adenine nucleotides on chloroplast coupling factor CF1. FEBS Lett 101: 316–320PubMedCrossRefGoogle Scholar
  121. Strotmann H, Bickel-Sandkötter S, Franek U and Gerke V (1981) Nucleotide interactions with membrane-bound CF1. In: R Selman and Selman-Reimer S (eds) Energy Coupling in Photosynthesis Research, pp 187–196. Elsevier, North HollandGoogle Scholar
  122. Strotmann H, Kleefeld S and Lohse D (1987) Control of ATP hydrolysis in chloroplasts. FEBS Lett 221: 265–269CrossRefGoogle Scholar
  123. Suss K-H (1986) Stable binding interaction among subunits of the chloroplast ATP synthase (CF1-CF0) as examined by solid support (nitrocellulose)-subunit reconstitution-immunoblotting. FEBS Lett 199: 169–172Google Scholar
  124. Walker JE, Saraste M, Runswick MJ and Gay N (1982) Distantly related sequences in the α-and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1: 945–951PubMedGoogle Scholar
  125. Wang JH (1988) Chemical modification of active sites in relation to the catalytic mechanism of F1. J Bioenerg Biomemb 20: 407–422Google Scholar
  126. Wetzel CM and McCarty RE (1993) Aspects of subunit interactions in the chloroplast ATP synthase: II. Characterization of a chloroplast coupling factor 1-subunit III complex from spinach thylakoids. Plant Physiol 102: 251–259PubMedGoogle Scholar
  127. Wimmer MJ and Rose IA (1977) Mechanism for oxygen exchange in the chloroplast photophosphorylation system. J Biol Chem 252: 6769–6775PubMedGoogle Scholar
  128. Wood JM, Wise JG, Senior AE, Futai M and Boyer PD (1987) Catalytic properties of the F1-adenosine triphosphatase from Escherichia coli K-12 and its genetic variants as revealed by O18 exchanges. J Biol Chem 262: 2180–2186PubMedGoogle Scholar
  129. Xue Z and Boyer PD (1989) Modulation of the GTPase activity of the chloroplast F1-ATPase by ATP binding at non-catalytic sites. Eur J Biochem 179: 677–681PubMedCrossRefGoogle Scholar
  130. Xue Z, Zhou J-M, Melese T, Cross RL and Boyer PD (1987a) Chloroplast F1-ATPase has more than three nucleotide binding sites, and 2-azido ADP or 2-azido ATP at both catalytic and noncatalytic sites labels the β subunit. Biochemistry 26: 3749–3753PubMedCrossRefGoogle Scholar
  131. Xue Z, Miller CG, Zhou J-M and Boyer PD (1987b) Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. FEBS Lett 223: 391–394PubMedCrossRefGoogle Scholar
  132. Zhou J-M and Boyer PD (1992) MgADP and free Pi as the substrates and the Mg2+ requirement for photophosphorylation. Biochemistry 31: 3166–3171PubMedGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Mark L. Richter
    • 1
  • Denise A. Mills
    • 1
  1. 1.Department of BiochemistryThe University of KansasLawrenceUSA

Personalised recommendations