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• Identification of a mitochondrial ATP synthase small subunit gene (RMtATP6) expressed in response to salts and osmotic stresses in rice (Oryza sativa L.). (Zhang, X., et al. (2005))
  
  
• Alkaline pH homeostasis in bacteria: New insights. (Padan, E., et al. (2005))
  
  
• The F(1)-ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function. (Schnaufer, A., et al. (2005))
  
  
• The role of the epsilon subunit in Escherichia coli ATP synthase: The C-terminal domain is required for efficient energy coupling. (Cipriano, D.J., and Dunn, S.D. (2005))
  
  
• Structural evidence for a constant c11 ring stoichiometry in the sodium F-ATP synthase. (Meier, T., et al. (2005))
  
  
• An alternative reaction pathway of F1-ATPase suggested by rotation without 80{degrees}/40{degrees} substeps of a sluggish mutant at low ATP. (Shimabukuro, K., et al. (2005))
  
  
• A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase. (Gao, Y.Q., et al. (2005))
  
  
• Vasoconstriction caused by the ATP synthase subunit-coupling factor 6: a new function for a historical enzyme. (Watts, S.W. (2005))
  
  
• Purification, crystallization, and properties of F(1)-ATPase complexes from the thermoalkaliphilic Bacillus sp. strain TA2.A1. (Stocker, A., et al. (2005))
  
  
• A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase. (Dudkina, N.V., et al. (2005))
  
  
• Differential gene expression during apoptosis induced by a serum factor: Role of mitochondrial F(0)-F(1) ATP synthase complex. (Dudkina, N.V., et al. (2005))
  
  
• Real-time Monitoring of Conformational Dynamics of the Epsilon Subunit in F1-ATPase. (Iino,R., et al. (2005))
  
  
• Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy. (Wilkens, S., et al. (2005))
  
  
• Inaugural article: making ATP. (Xing, J., et al. (2005))
  
  
• The c(15) ring of the Spirulina platensis F-ATP synthase: F(1)/F(0) symmetry mismatch is not obligatory. (Pogoryelov, D., et al. (2005))
  
  
• Function, structure, and biogenesis of mitochondrial ATP synthase. (Ackerman, S.H., and Tzagoloff, A. (2005))
  
  
• Regulation of the F(0)F(1)-ATP synthase: The conformation of subunit epsilon might be determined by directionality of subunit gamma rotation. (Feniouk, B.A., and Junge, W. (2005))
  
  
• Effects of site-directed mutation on the function of the chloroplast ATP synthase epsilon subunit. (Zeng, X., et al. (2005))
  
  
• Structure of dimeric mitochondrial ATP synthase: Novel F0 bridging features and the structural basis of mitochondrial cristae biogenesis. (Minauro-Sanmiguel F., et al. (2005))
  
  
• Mitochondrial ATP synthase residue beta-Arginine-408, which interacts with the inhibitory site of regulatory protein IF1, is essential for the function of the enzyme. (Ichikawa, N., et al. (2005))
  
  
• Both rotor and stator subunits are necessary for efficient binding of F1 to FO in functionally assembled E. coli ATP synthase. (Krebstakies, T., et al. (2005))
  
  
• Cyclical mitochondrial deltapsiM fluctuations linked to electron transport, F0F1 ATP-synthase and mitochondrial Na+/Ca+2 exchange are reduced in Alzheimer's disease cybrids. (Thiffault C., and Bennett J.P. Jr. (2005))
  
  
• Structure of the F(1)-binding Domain of the Stator of Bovine F(1)F(o)-ATPase and How it Binds an alpha-Subunit. (Carbajo R.J., et al. (2005))
  
  
• Subunit movement in individual H+-ATP synthases during ATP synthesis and hydrolysis revealed by fluorescence resonance energy transfer. (Borsch, M., and Graeber, P. (2005))
  
  
• Protein complexes in the archaeon methanothermobacter thermautotrophicus analyzed by blue native/SDS-PAGE and mass spectrometry. (Farhoud, M.H., et al. (2005))
  
  
• Substitutions of the conserved Gly47 affect the CF1 inhibitor and proton gate functions of the chloroplast ATP synthase epsilon subunit. (Dong, H., et al. (2005))
  
  
• Interactions of gammaT273 and gammaE275 with the beta Subunit PSAV Segment that Links the gamma Subunit to the Catalytic Site Walker Homology B Aspartate Are Important to the Function of Escherichia coli F₁Fo ATP Synthase. (Boltz, K.W., and Frasch, W.D. (2005))
  
  
• On the Gordon conference on Molecular and Cellular Bioenergetics (which I unfortunately missed) there were several interesting presentations on ATP synthase. See the conference web-site for details.
  
  
• The F₁Fo-ATP synthase of Mycobacterium smegmatis is essential for growth. (Tran, S.L., and Cook, G.M. (2005))
  
  
• The modification of the conserved GXXXG motif of the membrane-spanning segment of subunit G destabilizes the supramolecular species of yeast ATP synthase. (Bustos, D.M. and Velours, J.(2005))
  
  
• Effect of denaturants on multisite and unisite ATP hydrolysis by bovine heart submitochondrial particles with and without inhibitor protein. (de Gomez-Puyou, M.T., et al.(2005))
  
  
• Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase. (Ahmad, Z., and Senior, A.E.(2005))
  
  
• Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase. (Zimmermann, B., et al.(2005))
  
  
• Distances between the b-subunits in the tether domain of F(0)F(1)-ATP synthase from E. coli. (Steigmiller, S. et al.(2005))
  
  
• Manipulating the Length of the b Subunit F1 Binding Domain in F1F0 ATP Synthase from Escherichia coli. (Bhatt, D., et al. (2005))
  
  
• F1F0-ATP Synthase Complex Interactions In Vivo Can Occur in the Absence of the Dimer Specific Subunit e. (Gavin, P.D. et al. (2005))
  
  
• The yeast F1Fo-ATP synthase: Analysis of the molecular organization of subunit G and the importance of a conserved GXXXG motif. (Saddar, S., and Stuart, R.A. (2005))
  
  
• Interactions between betaD372 and gamma Subunit N-Terminus Residues gammaK9 and gammaS12 Are Important to Catalytic Activity Catalyzed by Escherichia coli F(1)F(o)-ATP Synthase. (Lowry, D.S. and Frasch, W.D. (2005))
  
  
• Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. (Meier, T., et al. (2005))
  
  
• ATP-dependent rotation of mutant ATP synthases defective in proton transport. (Hosokawa, H., et al. (2005))
  
  
• Rotary torque produced by proton motive force in FoF(1) motor. (Yunghao, Z., et al. (2005))
  
  
• The epsilon subunit of mitochondrial ATP synthase is required for normal spindle orientation during the Drosophila embryonic divisions. (Kidd, T., et al. (2005))
  
  
• Down-regulation of mitochondrial F1F0-ATP synthase in human colon cancer cells with induced 5-fluorouracil resistance. (Shin, Y.K., et al. (2005))
  
  
• Expression of bovine F1 ATPase with functional complementation in yeast saccharomyces cerevisiae. (Puri, N., et al. (2005))
  
  
• The inhibitor protein of the F(1)F(0)-ATP synthase is associated to the external surface of endothelial cells. (Cortes-Hernandez, P., et al. (2005))
  
  
• Assembly factors of F(1)F(o)-ATP synthase across genomes. (Pickova, A., et al. (2005))
  
  
• Activation of pausing F₁ motor by external force. (Hirono-Hara, Y., et al. (2005))
  
  
• N-terminal deletion of the gamma subunit affects the stabilization and activity of chloroplast ATP synthase. (Ni, Z.L., et al. (2005))
  
  
• Active oligomeric ATP synthases in mammalian mitochondria. (Krause, F., et al. (2005))
  
  
• Highly coupled ATP synthesis by F1-ATPase single molecules. (Rondelez, Y., et al.)
  
  
• Failure to assemble the alpha 3beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae. (Lefebvre-Legendre, L., et al.)
  
  
• Functional Analysis of Subunit e of the F1Fo-ATP Synthase of the Yeast Saccharomyces cerevisiae: Importance of the N-Terminal Membrane Anchor Region. (Everard-Gigot, V. et al.)
  
  
• Photo-induced proton gradients and ATP biosynthesis produced by vesicles encapsulated in a silica matrix. (Luo, T.J. et al.)
  
  
• Identification and differential accumulation of two isoforms of the CF(1)-beta subunit under high light stress in Brassica rapa. (Jiao, S., et al.)
  
  
• Mitochondrial ATP Synthase: A Bioinformatic Approach Reveals New Insights About the Roles of Supernumerary Subunits g and A6L. (Hong, S., and Pedersen, P.L.)
  
  
• ATP-driven stepwise rotation of FoF1-ATP synthase. (Ueno, H., at al.)
  
  
• Light-induced proton slip and proton leak at the thylakoid membrane. (Richter, M., et al.)
  
  
• Involvement of ATP synthase residues alphaArg-376, betaArg-182, and betaLys-155 in Pi binding. (Ahmad, Z., and Senior, A.E.)
  
  
• The binding mechanism of the yeast F1-ATPase inhibitory peptide. Role of catalytic intermediates and enzyme turnover. (Corvest, V., et al.)
  
  
• One Rotary Mechanism for F1-ATPase over ATP Concentrations from Millimolar down to Nanomolar. (Sakaki, N., et al.)
  
  
• Proton slip in the ATP synthase of Rhodobacter capsulatus: induction, proton conduction, and nucleotide dependence. (Feniouk, B.A., et al.)
  
  
• Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F(1)F(o) ATP synthase. (Ishmukhametov, R.R., et al.)
  
  
• P/O ratios of mitochondrial oxidative phosphorylation. (Hinkle, P.C.)
  
  
• Conformational change of H+-ATPase beta monomer revealed on segmental isotope labeling NMR spectroscopy. (Yagi, H., et al.)
  
  
• A Diarylquinoline Drug Active on the ATP Synthase of Mycobacterium tuberculosis. (Andries, K., et al.)
  
  
• ATP Synthase from Saccharomyces cerevisiae: Location of Subunit h in the Peripheral Stalk Region. (Rubinstein, J.L., et al.)
  
  
• Lipid raft proteome reveals ATP synthase complex in the cell surface. (Bae, T.J., et al.)
  
  
• Inhibition sites in F 1-ATPase from bovine heart mitochondria. (Gledhill J.R., and Walker J.E.)
  
  
• Inhibitory and Anchoring Domains in the ATPase Inhibitor Protein IF(1) of Bovine Heart Mitochondrial ATP Synthase. (Zanotti F., et al.)
  
  
• Bacterial Na+ - or H+ -coupled ATP synthases operating at low electrochemical potential. (Dimroth P, and Cook, G.M.)
  
  
• The stoichiometry of the chloroplast ATP synthase oligomer III in Chlamydomonas reinhardtii is not affected by the metabolic state. (Meyer Zu Tittingdorf J.M., et al.)
  
  
• In vitro and in vivo studies of F(0)F(1)ATP synthase regulation by inhibitor protein IF(1) in goat heart. (Di Pancrazio, F., et al.)
  
  
• Expression of the Drosophila melanogaster ATP synthase alpha subunit gene is regulated by a transcriptional element containing GAF and Adf-1 binding sites. (Talamillo A., et al.)
  
  
• F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane. ( van Bloois, E., et al.)
  
  
• The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H(+)/ATP coupling ratio. (Cross, R.L., and Muller V.)
  
  
• Three-Dimensional Structure of the Intact Thermus thermophilus H(+)-ATPase/Synthase by Electron Microscopy. (Bernal, R.A., and Stock, D.)
  
  
• Dimeric H(+)-ATP synthase in the chloroplast of Chlamydomonas reinhardtii. (Rexroth, S., et al.)
  
  
• pKa of the essential Glu54 and backbone conformation for subunit c from the H+-coupled F1F0 ATP synthase from an alkaliphilic Bacillus. (Rivera-Torres I.O., et al.)
  
  
• Observation of calcium-dependent unidirectional rotational motion in recombinant photosynthetic F1-ATPase molecules. (Tuckler, W.C., et al.)
  
  
• Age-dependent changes in the mitochondrial F(0)F(1) ATP synthase. (Guerrieri F., et al.)
  
  
• Rotary F-ATPase. (Muller, M., et al.)
  
  
• Ni-chelate-affinity purification and crystallization of the yeast mitochondrial F(1)-ATPase. (Mueller, D.M., et al.)
  
  
• Expression and purification of a novel rice (Oryza sativa L.) mitochondrial ATP synthase small subunit in Escherichia coli. (Liu, S., and Zhang, X.)
  
  
• The subunit b dimer of the FoF1-ATP synthase: Interaction with F1-ATPase as deduced by site-specific spin-labeling (Motz, C., et al.)
  
  
• Determination of Proton Flux and conductance at pH 6.8 through single Fo sectors from Escherichia coli. (Franklin, M.J., et al.)
  
  
• Solution structure of subunit f(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria. (Carbajo, R.J., et al.)
  
  
• Physiological Ligands ADP and P(i) Modulate the Degree of Intrinsic Coupling in the ATP Synthase of the Photosynthetic Bacterium Rhodobacter capsulatus. (Turina, P., et al.)
  
  
• Role of beta-Asn-243 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase. (Ahmad Z., and Senior A.E.)
  
  
• Thermophilic ATP synthase has a decamer c-ring: Indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling. (Mitome, N., et al.)
  
  
• Functional expression of hexahistidine-tagged beta-subunit of yeast F(1)-ATPase and isolation of the enzyme by immobilized metal affinity chromatography. (Ichikawa M., and Mizuno, N.)
  
  
• The ion channel of F-ATP synthase is the target of toxic organotin compounds. (Balmoos Cv.C., et al.)
  
  
• Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the escherichia coli F1F0 ATP synthase. (Yi, L., et al.)
  
  
• The modulation in subunit e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology. (Arselin, G., et al.)
  
  
• Reversible assembly of the ABC-transporter Mdl1 with the F₁Fo-ATP synthase in mitochondria. (Galluhn, D., and Langer, T.)
  
  
• The transmembrane domain of subunit b of the Escherichia coli FF ATP synthase is sufficient for H-translocating activity together with subunits a and c. (Greie, J.C., et al.)
  
  
• Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon methanococcus jannaschii visualized by electron microscopy. (Coskun, U., et al.)
  
  
• Real-Time pH Microscopy down to the Molecular Level by Combined Scanning Electrochemical Microscopy/Single-Molecule Fluorescence Spectroscopy. (Boldt F.M., et al.)
  
  
• Backbone (1)h, (15)n and (13)c assignments for the subunit a of the e. Coli ATP synthase. (Dmitriev, O.Y., et al.)
  
  
• A Normal Mode Analysis of Structural Plasticity in the Biomolecular Motor F(1)-ATPase. (Cui, Q., et al.)
  
  
• Rotor/stator interactions of the epsilon subunit in E. coli ATP synthase and implications for enzyme regulation. (Bulygin, V.V., et al.)
  
  
• The Proton-Driven Rotor of ATP Synthase: Ohmic Conductance (10 fS), and Absence of Voltage Gating. (Feniouk, B.A, et al.)
  
  
• ATP synthase that lacks Fo a subunit; isolation, properties and indication of Fob2subunits as an anchor-rail of rotating c-ring. (Ono, S., et al.)
  
  
• How proton translocation across mitochondrial inner membranes drives the Fo rotor of ATP synthase. (McCabe, M.G., et al.)
  
  
• Mitochondrial ATP synthasome three dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. (Chen, C., et al.)
  
  
• Genetic complementation between mutant b subunits in F1F0 ATP synthase. (Grabar, T.B., Cain, B.D.)
  
  
• A Column Centrifugation Method for the Reconstitution in Liposomes of the Mitochondrial F0F1 ATP Synthase/ATPase (Vazquez-Contreras, E., et al.)
  
  
• Uniformly oriented bacterial F0F1-ATPase immobilized on a semi-permeable membrane: a step towards biotechnological energy transduction. (Bhattacharya, S., et al.)
  
  
• Mutagenesis of residue beta-Arg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase. (Ahmad, Z., and Senior, A.E.)
  
  
• Cross-linking ATP synthase complexes in vivo eliminates mitochondrial cristae. (Gavin, P.D., et al.)
  
  
• A novel role of Mgm1p in ATP synthase assembly and cristae formation/maintenance. (Amutha, B., et al.)
  
  
• Significance of the subunit in the thiol modulation of chloroplast ATP synthase. (Konno, H., et al.)
  
  
• Binding of single nucleotides to H(+)-ATP synthases observed by fluorescence resonance energy transfer. (Steigmiller, S., et al.)
  
  
• F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis. (Van Der Laan, M., et al.)
  
  
• Mechanisms of ATPases--a multi-disciplinary approach. (Rappas, M., et al.)
  
  
• F1Fo-ATP synthase. Analysis of sequence determinants in the N-terminal region of alpha subunit for binding of delta subunit. (Weber J., et al.)
  
  
• Fluorescent probes applied to catalytic cooperativity in ATP synthase. ( Weber J., and Senior A.E.)
  
  
• Regulatory role of the C-terminus of the epsilon subunit from the chloroplast ATP synthase. (Nowak K.F., and McCarty R.E.)
  
  
• Replacement of amino acid sequence features of a- and c-subunits of ATP synthases of alkaliphilic bacillus with the bacillus consensus sequence results in defective oxidative phosphorylation and non-fermentative growth at pH 10.5. (Wang, Z., et al.)
  
  
• Lysine 43 is trimethylated in subunit c from bovine mitochondrial ATP synthase and in storage bodies associated with Batten disease. (Chen, R., et al.)
  
  
• Escherichia coli proton-translocating F(0)F(1)-ATP synthase and its association with solute secondary transporters and/or enzymes of anaerobic oxidation-reduction under fermentation. (Trchounian A.)
  
  
• Small molecule mitochondrial F1F0 ATPase hydrolase inhibitors as cardioprotective agents. Identification of 4-(N-arylimidazole)-substituted benzopyran derivatives as selective hydrolase inhibitors. (Atwal K.S., et al.)
  
  
• Insights into the Molecular Mechanism of Rotation in the F(o) Sector of ATP Synthase. (Aksimentiev, A., et al.)
  
  
• Asymmetry in the F(1)-ATPase and Its Implications for the Rotational Cycle. (Sun, S.X., et al.)
  
  
• Respiratory chain complex V deficiency due to a mutation in the assembly gene ATP12. (De Meirleir, L., et al.)
  
  
• Inverse regulation of rotation of F1-ATPase by the mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase. (Ueoka-Nakanishi, H., et al.)
  
  
• Molecular evolution of the modulator of chloroplast ATP synthase: origin of the conformational change dependent regulation. (Hisabori, T., et al.)
  
  
• Mechanically driven ATP synthesis by F1-ATPase. (Itoh, H., et al.)
  
  
• Binding of the b-Subunit in the ATP Synthase from Escherichia coli. (Diez, M., et al.)
  
  
• Overexpression, purification, and characterization of human and bovine mitochondrial ATPase inhibitors: comparison of the properties of mammalian and yeast ATPase inhibitors. (Ichikawa N., and Ogura, C.)
  
  
• Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain. (Hardy, A.W., et al.)
  
  
• Cloning and molecular characterization of the atp operon encoding for the F(1)F(0)-ATP synthase from a thermoalkaliphilic Bacillus sp. strain TA2.A1. (Keis, S., et al.)
  
  
• Proton-powered subunit rotation in single membrane-bound F(0)F(1)-ATP synthase. (Diez, M., et al.)
  
  
• Energy-dependent transformation of Fo2F1-ATPase in Paracoccus denitrificans plasma membranes. (Vinogradov A.D., and Zharova T.V.)
  
  
• Quantitative determination of direct binding of b subunit to F1 in Escherichia coli F1F0-ATP synthase. (Weber, J., et al.)
  
  
• Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. (Dmitriev, O.Y., et al.)
  
  
• Computer simulation of cytoplasmic pH regulation mediated by the F-type H(+)-ATPase. (Kobayashi, H.)
  
  
• Each yeast mitochondrial F(1)F(0)-ATP synthase complex contains a single copy of subunit 8. (Stephens, A.N., et al.)
  
  
• FRET reveals changes in the F(1)-stator stalk interaction during activity of F(1)F(0)-ATP synthase. (Gavin, P.D., et al.)
  
  
• Catalysis and rotation of F1 motor: Cleavage of ATP at the catalytic site occurs in 1 ms before 40{degrees} substep rotation. (Shimabukuro, K., et al.)
  
  
• Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase. (Strajbl, M., et al.)
  
  
• Electrical power fuels rotary ATP synthase. (Dimroth, P., et al.)
  
  
• Characterisation of subunit III and its oligomer from spinach chloroplast ATP synthase. (Poetsch, A., et al.)
  
  
• Structure of the mitochondrial ATP synthase by electron cryomicroscopy. (Rubinstein, J.L., et al.)
  
  
• Mechanics of coupling proton movements to c-ring rotation in ATP synthase. (Fillingame, R.H., et al.)
  
  
• Proton-Translocating ATP-Synthase of Paracoccus denitrificans: ATP-Hydrolytic Activity. (Zharova, T.V., and Vinogradov, A.D.)
  
  
• Rotary movements within the ATP synthase do not constitute an obligatory element of the catalytic mechanism. (Berden, J.A.)
  
  
• The Escherichia coli F₁F_O ATP synthase displays biphasic synthesis kinetics (Tomashek, J.J., et al.)
  
  
• Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane. (Angevine, C.M., et al.)
  
  
• Charge displacements during ATP-hydrolysis and synthesis of the Na⁺-transporting F_OF₁-ATPase of Ilyobacter tartaricus. (Burzik, C., et al.)
  
  
• The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit {delta} (Duvezin-Caubet, S., et al.)
  
  
• Inactivation of the chloroplast ATP synthase gamma subunit results in high non-photochemical fluorescence quenching and altered nuclear gene expression in Arabidopsis thaliana. (Dal Bosco, C. et al.)
  
  
• Topological and functional study of subunit h of the F1Fo ATP synthase complex in yeast Saccharomyces cerevisiae. (Fronzes, R. et al.)
  
  
• Interactions between Gamma R268, Gamma Q269 and the Beta subunit catch-Loop of E. coli F1 ATPase are Important for catalytic activity. (Greene M.D., and Frasch W.D.)
  
  
• On the Mechanism of ATP Hydrolysis in F(1)-ATPase. (Dittrich, M., et al.)
  
  
• Interference of methyl trachyloban-19-oate ester with CF(0) of spinach chloroplast H(+)-ATPase (Hernandez-Terrones M.G., et al.)
  
  
• The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli. (DeLeon-Rangel J., et al.)
  
  
• Uniformly oriented immobilized bacterial F 0F 1 ATPase on semi-permeable membrane: A step towards biotechnological energy transduction. (Bhattacharya, S., et al.)
  
  
• Knock-Out of the Genes Coding for the Rieske Protein and the ATP-Synthase delta-Subunit of Arabidopsis. Effects on Photosynthesis, Thylakoid Protein Composition, and Nuclear Chloroplast Gene Expression (Maiwald, D., et al.)
  
  
• YidC Is Strictly Required for Membrane Insertion of Subunits a and c of the F(1)F(0)ATP Synthase and SecE of the SecYEG Translocase. (Yi. L., et al.)
  
  
• Clostridium pasteurianum F(1)F(o) ATP Synthase: Operon, Composition, and Some Properties. (Das A., and Ljungdahl, L.G.)
  
  
• The structure of bovine F(1)-ATPase in complex with its regulatory protein IF(1). (Cabezon, E., et al.)
  
  
• A tenth atp gene and the conserved atpI gene of a Bacillus atp operon have a role in Mg2+ uptake. (Hicks, D.B., et al.)
  
  
• ATP synthases: insights into their motor functions from sequence and structural analyses. (Hong S., and Pederson, P.L.)
  
  
• FoF1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance. (Suzuki T. et al.)
  
  
• Purification and biochemical characterization of the F1Fo-ATP synthase from thermoalkaliphilic Bacillus sp. strain TA2.A1. (Cook G.M. et al.)
  
  
• Over-expression of Escherichia coli F1F(o)-ATPase subunit a is inhibited by instability of the uncB gene transcript. (Arechaga I. et al.)
  
  
• Integration of b subunits of unequal lengths into F1F0 ATP synthase. (Grabar T.B., and Cain B.D.)
  
  
• Isolated epsilon subunit of thermophilic F1-ATPase binds ATP. (Kato-Yamada Y., and Yoshida M.)
  
  
• Gene clusters encoding ATP synthase of Haloarcula japonica strain TR-1. (Yatsunami R., et al.)
  
  
• The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. (Gilkerson R.W., et al.)
  
  
• The Mechanism of ADP Phosphorylation by ATP Synthase. (Weber, J.)
  
  
• Investigation of the Role and Mechanism of IF1 and STF1 Proteins, Twin Inhibitory Peptides Which Interact with the Yeast Mitochondrial ATP Synthase. (Venard, R., et al.)
  
  
• Molecular evolution of the modulator of chloroplast ATP synthase: origin of the conformational change dependent regulation. (Hisabori, T., et al.)
  
  
• ATP synthesis driven by proton transport in F(1)F(0)-ATP synthase (Weber, J., and Senior, A.E.)
  
  
• Isolation of a complete A(1)A(O) ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii. (Lingl, A., et al.)
  
  
• The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains. (Lolkema J.S., and Boekema E.J.)
  
  
• Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). (Leyva J.A., et al.)
  
  
• Direct interaction of subunits a and b of the F0 complex of Escherichia coli ATP synthase by forming an ab2 subcomplex.(Stalz, W.D., et al.)
  
  
• The enigmatic mitochondrial ORF ymf39 codes for ATP synthase chain b.(Burger, G., et al.)
  
  
• The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATPsynthase complex in the mitochondrial membrane.(Arselin, G., et al.)
  
  
• The products of the mitochondrial orf25 and orfB genes are F(O) components in the plant F(1)F(O) ATP synthase.(Heazlewood, J.L., et al.)
  
  
• pH-dependent Ca2+ binding to the F0 c-subunit affects proton translocation of the ATP synthase from Synechocystis 6803.(Van Walraven H.S., et al.)
  
  
• Introduction of a carboxyl group in the loop of the F0 c-subunit affects the H+/ATP coupling ratio of the ATP synthase from Synechocystis 6803.(Van Walraven H.S., et al.)
  
  
• Cross-linking of the endogenous inhibitor protein (IF1) with rotor (gamma, epsilon) and stator (alpha) subunits of themitochondrial ATP synthase.(Minauro-Sanmiguel, F.)
  
  
• Subunit rotation of vacuolar-type proton pumping ATPase: Relative rotation of the G as to c subunit.(Hirata, T., et al.)
  
  
• Abstract Subunit E of mitochondrial ATP synthase: a bioinformatic analysis reveals a phosphopeptide binding motif supporting a multifunctional regulatory role and identifies a related human brain protein with the same motif.(Hong S,and Pedersen P.L.)
  
  
• ORFB is a subunit of F(1)F(O)-ATP synthase: insight into the basis of cytoplasmic male sterility in sunflower.(Sabar M., et al.)
  
  
• Rotary protein motors.(Oster G., and Wang H.)
  
  
• The molecular neighborhood of subunit 8 of yeast mitochondrial F1FO-ATP synthase probed by cysteine scanning mutagenesis andchemical modification.(Stephens A.N., et al.)
  
  
• F0 cysteine, bCys21, in the Escherichia coli ATP synthase is involved in regulation of potassium uptake and molecular hydrogen production in anaerobic conditions.(Mnatsakanyan N., et al.)
  
  
• Association of atp synthase alpha-chain with neurofibrillary degeneration in alzheimer's disease.(Sergeant, N, et al.)
  
  
• Transcriptional Regulation of the Nuclear Gene Encoding the alpha-Subunit of the Mammalian Mitochondrial F(1)F(0) ATP Synthase Complex: Role for the Orphan Nuclear Receptor, COUP-TFII/ARP-1.(Jordan, E.M.,et al.).
  
  
• Evidence for rotation of V1-ATPase.(Imamura H., et al.)
  
  
• Dose-dependent inhibition of mitochondrial ATP synthase by 17 beta-estradiol.(Massart F.,et al.).
  
  
• Conformational change of the chloroplast ATP synthase on the enzyme activation processdetected by the trypsin sensitivity of the gamma subunit.(Sugiyama K., and Hisabori T.).
  
  
• Mitochondrial ATP synthasome: Cristae enriched membranes and a multiwelldetergent screening assay yield dispersed single complexes containing theATP synthase and carriers for Pi and ADP/ATP1 (Ko YH, et al.).
  
  
• Identification of the F1-binding surface on the delta-subunit of ATP synthase(Weber J, et al.).
  
  
• H(+)/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF(0)F(1)-liposomes (Turina P, et al.).
  
  
• Sodium ion cycling mediates energy coupling between complex I and ATP synthase. (Gemperli AC, et al.)
  
  
• Proteome analysis reveals phosphorylation of ATP synthase beta -subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes. (Hojlund K, et al.)
  
  
• Complete DNA sequence of the atp operon of the sodium-dependent F(1)F(o) ATP synthase from Ilyobacter tartaricus and identification ofthe encoded subunits (Meier T, et al.)
  
  
• Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli. (Zhang D., Vik S.B.)
   
  
• Helix Packing in Subunit a of the Escherichia coli ATP Synthase as Determined by Chemical Labeling and Proteolysis of the Cysteine-Substituted Protein (Zhang D., Vik S.B.)
  
  
•  Ectopic beta-chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis (Martinez L.O., et al.).
  
  
• The proton channel is the minimal structure of ATP synthasenecessary and sufficient for microcin h47 antibiotic action (Rodriguez E., and Lavina M.).
  
  
• The C-Terminal Domain of the epsilon Subunit of the Chloroplast ATP Synthase Is Not Required for ATP Synthesis (Nowak KF, et al.)
  
  
• Aqueous access channels in subunit a of rotary ATP synthase (Angevine CM, and Fillingame RH.,)
  
  
• The H(+)-ATPase from chloroplasts: effect of differentreconstitution procedures on ATP synthesis activity and on phosphatedependence of ATP synthesis (Grotjohann I, Graber P.).
  
  
• Dimerization of F(0)F(1)ATP synthase from bovine heartis independent from the binding of the inhibitor protein IF(1) (Tomasetig L, et al.).
  
  
• F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring (Suzuki, T. et al.).
  
  
• From chloroplasts to photosystems: in situ scanningforce microscopy on intact thylakoid membranes. (Kaftan D, et al.). Density of the ATP synthase molecules in chloroplasts determined.
  
  
• Membrane embedded location of Na⁺ or H⁺ binding sites on the rotor ring of F₁F_O ATP synthases. (Von Ballmoos C., et al.)
  
  
• Subunit gamma -GFP fusions are functionallyincorporated into mitochondrial F₁F_O ATPsynthase arguing against a rigid cap structure at the top of F₁. (Prescott M. et al)
  
  
• Structural model of the transmembrane F(o) rotary sector of H(+)-transporting ATP synthase derived by solutionNMR and intersubunit cross-linking in situ. (Fillingame R.H., and Dmitriev O.Y.)
  
  
• Dimerization of F₀F₁ ATP synthase from bovine heart is independent from the binding of the inhibitor protein IF₁. (Tomasetig L., et al.)
  
  
• The H⁺-ATPase from chloroplasts:effect of different reconstitution procedures on ATP synthesisactivity and on phosphate dependence of ATP synthesis (Grotjohann, I., and Gräber, P.)
  
  
• Complete inhibition of the tentoxin resistant F1-ATPase from Escherichia coli by the phytopathogenic inhibitor tentoxin after substitution of critical residues inthe alpha - and beta -subunit. (Schnick C., et al., full text PDF is available)
  
  
• Improved purification for thermophilic F₁F_O ATP synthase using n-dodecyl beta-D-maltoside. (Hazard A, and Montemagno, C.)
  
  
• Sulfite inhibits the F₁F_O-ATP synthase and activates the F₁F_O-ATPase of Paracoccus denitrificans.(Pacheco-Moises F., et al.)
  
  
• Binding affinities and protein ligand complex geometries of nucleotides at the F(1) part of the mitochondrial ATP synthase obtained by ligand docking calculations. (Steinbrecher T, et al.)
  
  
• ATP Synthase from Saccharomyces cerevisiae: Location of the OSCP Subunit in the Peripheral Stalk Region.(Rubinstein, J., and Walker, J.)
  
  
• Papers in "Plant Physiology" journalare now included in Entrez database. Some interesting papers of 1993-2002, mostly on the chloroplast ATP synthase can be found there.
  
  
• Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase.
  (Vonck J, et al.)
  
  
• Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring. (Nishio K, et al.)
  
  
• Factor B is essential for ATP synthesis by mitochondria. (Belogrudov G.)
  
  
• Structures and Interactions of Proteins Involved in the Coupling Function of the Protonmotive F(o)F(1)-ATP Synthase. (Gaballo A. et al.)
  
  
• The 12th EBEC conference heldon 10th-16th September, 2002 in Arcachon had some ratherinteresting posters on ATP synthase (Here is a .PDF file with abstracts and the special 12th EBEC issue of BBA-Bioenergetics). To name just a few:

1. Rotation in the F₁ was shown by FRET (Fluorescence Resonance Energy Transfer): two fluorescent dyes were bound to the enzyme (one at rotor, one at stator). A nice three-step pattern was observed upon ATP synthesis (!) and hydrolysis. Abstract A4, Michael Börsch et al.
2. Wolfgang Junge in his lecture presented experimental data suggesting that during catalysis the "upper region" (12 C-terminal  aminoacid residues) of gamma subunit  i) can be cross-linked with alpha subunit without the loss of activity; ii) can be cut off without the loss of activity. One of the possible explanations proposed was that the rotation of gamma subunit is around covalent bond of the polypeptide chain below the C-terminal region, while this region itself is fixed in the alpha ₃ beta ₃  "crown" of the enzyme. (Müller, M. et al)
3. Molecular mechanism of ATP synthesis was further refined by Alan Senior and Joahim Weber.  Abstract A44.
   

• New review on ATP synthase from P. Boyer inJBC: A research journey with ATP synthase. [Full-text PDF is here]
  
  
• Sodium ATP synthase: DCCD-sensitive rotation in a fully coupled enzyme shown with polarization-resolved confocal microscopy both for synthesis and hydrolysis.  (Kaim, G. et al., 2002, full-text PDF available)
  
  
• Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface. (Fillingame et al., full-text PDF available)
  
  
• Sodium ATP synthase: Molecular Mechanism ofthe ATP Synthase's F(o) Motor Probed by Mutational Analysesof Subunit a. (Wehrle et al., 2002)
  

• Homologous and heterologous inhibitory effects of ATPase inhibitor proteins on F-ATPases. (Cabezon, E. et al., 2002)
  

• The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain. (Del Rizzo P.A. et al., 2002)
  

• Subunit i of the yeast mitochondrial enzymeis linking ATP synthase molecules in dimmers (Paumard, P. et al., 2002)

• Yeast mitochondrial enzyme: ATP synthase trends to oligomerise. Subunit g and the first transmembranesegment of subunit b are important for this process, althoughtheir abscense does not alter oxydative phosphorylation (