Summary
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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
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: 1775–1780
Abrahams JP, Leslie AGW, Lutter R and Walker JE (1994) Structure at 2.8Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621–628
Admon A and Hammes GG (1987) Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1. Biochemistry 26: 3193–3197
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: 61–68
Andralojc PJ and Harris DA (1992) Isolation and characterization of a functional αβ heterodimer from ATP synthase of Rhodospirillum rubrum. FEBS Lett 310: 187–192
Anthon GE and Jagendorf AT (1986) Evidence for multiple effects in methanol activation of chloroplast coupling factor 1. Biochim Biophys Acta 848: 92–98
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: 7067–7072
Avron M and Jagendorf AT (1959) Evidence concerning the mechanism of adenine triphosphate formation by spinach chloroplasts. J Biol Chem 234: 967–972
Bakker-Grunwald T and van Dam K (1974) On the mechanism of activation of the ATPase in chloroplasts. Biochim Biophys Acta 347: 290–298
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: 68–72
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: 467–478
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: 233–238
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: 97–104
Beharry S and Bragg PD (1992) E. coli F1-ATPase can use GTP-nonchaseable bound adenine nucleotide to synthesize ATP in DMSO. Biochemistry 31: 11472–11476
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: 151–156
Berg HC (1975) Bacterial behavior. Nature 254: 389–392
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: 21197–21201
Bickel-Sandkötter S and Strotmann H (1981) Nucleotide binding and regulation of chloroplast ATP synthase. FEBS Lett 125: 188–192
Boyer PD (1987) The unusual enzymology of ATP synthase. Biochemistry 26: 8503–8507
Boyer PD (1993) The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim Biophys Acta 1140: 215–250
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, Amsterdam
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: 1534–1538
Bruist MF and Hammes GG (1981) Further characterization of nucleotide binding sites on chloroplast coupling factor one. Biochemistry 20: 6298–6305
Bruist MF and Hammes GG (1982) Mechanism for catalysis and regulation of adenosine 5′-triphosphate hydrolysis by chloroplast coupling factor. Biochemistry 21: 3370–3377
Carlier MF and Hammes GG (1979) Interaction of nucleotides with chloroplast coupling factor 1. Biochemistry 18: 3446–3451
Cerione RA and Hammes GG (1982) Structural mapping of nucleotide binding sites on chloroplast coupling factor. Biochemistry 21: 745–752
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: 5773–5778
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: 11497–11501
Chen Z, Wu I and Richter ML (1992) Over-expression and refolding of β-subunit from chloroplast ATP synthase. FEBS Lett 298: 69–73
Colvert KC, Mills DA and Richter ML (1992) Structural mapping of cysteine-63 of the chloroplast ATP synthase β subunit. Biochemistry 31: 3930–3935
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: 201–208
Cross RL (1981) The mechanism and regulation of ATP synthesis by F1-ATPases. Ann Rev Biochem 50: 681–714
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: 395–406
Cross RL (1992). The reaction mechanism of F0F1-ATPsynthases. In: Ernster L (ed) Molecular Mechanisms in Bioenergetics pp 317–330. Elsevier, Amsterdam
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: 2874–2881
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: 5715–5719
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: 6192–6203
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: 453–461
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: 4901–4907
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: 213–218
Fromme P and Gräber P (1990a) Activation/inactivation and unisite catalysis by the reconstituted ATP-synthase from chloroplasts. Biochim Biophys Acta 1016: 29–42
Fromme P and Gräber P (1990b) ATP-hydrolysis in chloroplasts: Uni-site catalysis and evidence for heterogeneity of sites. Biochim Biophys Acta 1020: 187–194
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: 9763–9769
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: 14690–14695
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: 9585–9589
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: 426–440
Gresser MJ, Meyers JA and Boyer PD (1982) Catalytic site cooperativity of beef heart mitochondrial F1-ATPase. J Biol Chem 257: 12030–12038
Gromet-Elhanan Z (1992) Identification of the subunits required for the catalytic activity of the F1-ATPase. J Bioenerg Biomemb 24: 447–452
Gromet-Elhanan Z and Avital S (1992) Properties of the catalytic (αβ)-core complex of chloroplast CF1-ATPase. Biochim Biophys Acta 1102: 379–385
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: 1022–1028
Grubmeyer C, Cross RL and Penefsky HS (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. J Biol Chem 257: 12092–12100
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: 187–190
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: 3164–3170
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: 3646–3650
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: 3656–3664
Harris DA (1993) The ‘non-exchangeable’ nucleotides of F1-F0 ATP synthase; Cofactors in hydrolysis? FEBS Lett 316: 209–215
Harris DA and Crofts AR (1978) The initial stages of photophosphorylation: Studies using excitation by saturating, short flashes of light. Biochim Biophys Acta 502: 87–102
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: 335–348
Hiller R and Carmeli C (1985) Cooperativity among manganese-binding sites in the H-ATPase of chloroplasts. J Biol Chem 260: 1614–1617
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: 4551–4556
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: 6287–6292
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
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: 8536–8540
Huchzermeyer B (1988a) Nucleotide binding and ATPase activity of membrane bound chloroplast coupling factor (CF1). Z Naturforsch 43: 133–139
Huchzermeyer B (1988b) Phosphate binding to isolated chloroplast coupling factor (CF1). Z Naturforsch 43: 213–218
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: 245–250
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: 645–661
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: 1950–1953
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: 2486–2491
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: 11377–11383
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: 10–14
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: 12544–12549
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: 10881–10886
Komatsu-Takaki M (1989) Energy-dependent conformational changes in the epsilon subunit of the chloroplast ATP synthase. J Biol Chem 264: 17750–17753
Larson EM and Jagendorf AT (1986) Anion stimulation of ATPase in activated spinach chloroplast coupling factor 1 (CF1); Light activation mimic? Plant Physiol 80: S251
Leckband D and Hammes GG (1987) Interactions between nucleotide binding sites on chloroplast coupling factor 1 during ATP hydrolysis. Biochemistry 26: 2306–2312
Leckband D and Hammes GG (1988) Function of tightly bound nucleotides on membrane-bound chloroplast coupling factor. Biochemistry 27: 3629–3633
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: 278–284
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: 85–93
Magnusson RP and McCarty RE (1976) Light-induced exchange of nucleotides into coupling factor 1 in spinach chloroplast thylakoids. J Biol Chem 251: 7417–7422
McCarty RE and Fagan J (1973) Incorporation of N-ethylmaleimide into coupling factor 1 in spinach chloroplasts. Biochemistry 12: 1503–1507
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: 90–93
Milgrom YM and Murataliev MB (1987) Characterization of the nucleotide tight-binding sites of the isolated mitochondrial F1-ATPase. FEBS Lett 219: 156–160
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: 18725–18728
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: 11551–11558
Mills DA and Richter ML (1991) Nucleotide binding to the isolated β subunit of the chloroplast ATP synthase. J Biol Chem 266: 7440–7444
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: 6100–6108
Moroney JV and McCarty RE (1979) Reversible uncoupling of photophosphorylation by a new bifunctional maleimide. J Biol Chem 254: 8951–8955
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: 5915–5920
Nalin CM and Nelson N (1987) Structure and biogenesis of chloroplast coupling factor CF0CF1-ATPase. Curr Top Bioenerg 15: 273–294
Nalin CM, Snyder B and McCarty RE (1985) Selective modification of an α subunit of chloroplast coupling factor 1. Biochemistry 24: 2318–2324
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: 7657–7662
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: 9196–9201
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: 173–214
Philosoph S, Binder A and Gromet-Elhanan Z (1977) Coupling factor ATPase complex of R. rubrum. J Biol Chem 252: 8747–8752
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: 15037–15040
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: 7371–7373
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: 5755–5763
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: 12109–12113
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: 10654–10661
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: 1–8
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: 718–725
Roy H and Moudrianakis EN (1971) Interactions between ADP and the coupling factor of photophosphorylation. Proc Natl Acad Sci USA 68: 2720–2724
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: 4453–4459
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 Holland
Schumann J (1984) A study on the exchange of tightly bound nucleotides on the membrane-associated chloroplast ATP synthase complex. Biochim Biophys Acta 766: 334–342
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: 11817–11830
Shapiro AB and McCarty RE (1990) Substrate binding-induced alteration of nucleotide binding site properties of chloroplast coupling factor 1. J Biol Chem 265: 4340–4347
Shapiro AB and McCarty RE (1991) Four tight nucleotide binding sites of chloroplast coupling factor 1. J Biol Chem 266: 4194–4200
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: 17276–17285
Shavit N, Skye GE and Boyer PD (1967) Occurrence and possible mechanism of 32P and 18O exchange reactions of photophosphorylation. J Biol Chem 242: 5125–5130
Sherman PA and Wimmer MJ (1982) Two types of kinetic regulation of the activated ATPase in the chloroplast photophosphorylation system. J Biol Chem 257: 7012–7017
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: 539–543
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: 8801–8807
Snyder B and Hammes GG (1984) Structural mapping of chloroplast coupling factor. Biochemistry 23: 5787–5795
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: 10348–10354
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: 3884–3890
Stroop SD and Boyer PD (1985) Characteristics ofthe chloroplast ATP synthase as revealed by reaction at low ADP concentrations. Biochemistry 24: 2304–2310
Strotmann H, Bickel S and Huchzermeyer B (1976) Energy-dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF1. FEBS Lett 61: 194–198
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: 316–320
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 Holland
Strotmann H, Kleefeld S and Lohse D (1987) Control of ATP hydrolysis in chloroplasts. FEBS Lett 221: 265–269
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: 169–172
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: 945–951
Wang JH (1988) Chemical modification of active sites in relation to the catalytic mechanism of F1. J Bioenerg Biomemb 20: 407–422
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: 251–259
Wimmer MJ and Rose IA (1977) Mechanism for oxygen exchange in the chloroplast photophosphorylation system. J Biol Chem 252: 6769–6775
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: 2180–2186
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: 677–681
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: 3749–3753
Xue Z, Miller CG, Zhou J-M and Boyer PD (1987b) Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. FEBS Lett 223: 391–394
Zhou J-M and Boyer PD (1992) MgADP and free Pi as the substrates and the Mg2+ requirement for photophosphorylation. Biochemistry 31: 3166–3171
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Kluwer Academic Publishers
About this chapter
Cite this chapter
Richter, M.L., Mills, D.A. (1996). The Relationship Between the Structure and Catalytic Mechanism of the Chloroplast ATP Synthase. In: Ort, D.R., Yocum, C.F., Heichel, I.F. (eds) Oxygenic Photosynthesis: The Light Reactions. Advances in Photosynthesis and Respiration, vol 4. Springer, Dordrecht. https://doi.org/10.1007/0-306-48127-8_24
Download citation
DOI: https://doi.org/10.1007/0-306-48127-8_24
Publisher Name: Springer, Dordrecht
Print ISBN: 978-0-7923-3683-9
Online ISBN: 978-0-306-48127-7
eBook Packages: Springer Book Archive