Die gekoppelte Rotation der beiden Motoren einer einzelnen F0F1-ATP Synthase: Elastische Energiespeicherung während ATP Synthese und Hydrolyse

• Antragsteller: Professor Dr. Michael Börsch
• Fachliche Zuordnung: Biophysik
• Förderung: Förderung von 2005 bis 2009
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 5451896

• Erstellungsjahr: 2009

Zusammenfassung der Projektergebnisse

Keine Zusammenfassung vorhanden

Projektbezogene Publikationen (Auswahl)

• Asymmetry of rotational catalysis of single membrane-bound F0F1-ATP synthase (2005) Proc. SPIE 5699, 175-188
  N. Zarrabi, B. Zimmermann, M. Diez, P. Gräber, J. Wrachtrup, M. Börsch
  
• Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding (2005) FEBS Lett. 579, 1961-1967
  Armbrüster, C. Hohn, A. Hermesdorf, K. Schumacher, M. Börsch, G. Grüber
  
• 3D- localization of the a-subunit in FoF1-ATP synthase by time resolved single-molecule FRET (2006) Prog. Biomed. Optics Imag. - Proc. SPIE 6092, 60920H
  M. Düser, Y. Bi , N. Zarrabi , B. Zimmermann, S.D. Dunn, M. Börsch
  
• Crystal structure of the archaeal A1AO ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1AO subunits A and B (2006) J Mol Biol 358, 725-740
  Schäfer, S. M. Bailer, M. G. Düser, M. Börsch, R. A. Bernal, D. Stock, G. Grüber
  
• Proton-driven subunit rotation within a single ATP synthase (2006) in: ‘Proceedings of the VIII. Linz Winterworkshop - Advances in Single Molecule Research for Biology and Nanoscience’ (Eds. P. Hinterdorfer, G. Schütz, P. Pohl), pp. 13-18, Trauner Verlag Linz, ISBN 3-85499-163-0
  M. G. Düser, N. Zarrabi, Y. Bi, S. D. Dunn, M. Börsch
  
• Detecting substeps in the rotary motors of FoF1-ATP synthase by Hidden Markov Models (2007) Prog. Biomed. Optics Imag. - Proc. SPIE 6444, 64440E
  N. Zarrabi, M. G. Düser, R. Reuter, S. D. Dunn, J. Wrachtrup, M. Börsch
  
• Engineering the Structural Properties of DNA Block Copolymer Micelles by Molecular Recognition (2007) Angew. Chem. Int. Ed. 46, 1172-1175
  K. Ding, F. E. Alemdaroglu, M. Börsch, R. Berger, A. Herrmann
  
• Monitoring proton-driven rotation within a single biolgical nanomotor FoF1-ATP synthase (2007) Tissue Engineering 13, 867
  M. Börsch
  
• Monitoring the rotary motors of single FoF1-ATP synthase by synchronized multi channel TCSPC (2007) Proc. SPIE 6771, 67710F
  N. Zarrabi, M. G. Düser, S. Ernst, R. Reuter, S. D. Dunn, G. D. Glick, J. Wrachtrup, M. Börsch
  
• Controling the size of nanoparticles by an enzymatic reaction (2008) Angew. Chem. Int. Ed. 47, 974-976
  F. E. Alemdaroglu, J. Wang, M. Börsch, R. Berger, A. Herrmann
  
• Exploiting the nitrilotriacetic acid moiety for biolabeling with ultrastable perylene dyes (2008) J. Am. Chem. Soc. 130, 5398-5399
  K. Peneva, G. Mihov, A. Herrmann, N. Zarrabi, M. Börsch, T. M. Duncan, K. Müllen
  
• Quantum dots for singlepair fluorescence resonance energy transfer in membrane-integrated EF0F1 (2008) Biochem. Soc. Trans. 36, 1017-1021
  E. Galvez, M.G. Düser, M. Börsch, J. Wrachtrup, P. Gräber
  
• Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly (2008) Biochem. Soc. Trans. 36, 1027-1031
  M. Diepholz, M. Börsch, B. Böttcher
  
• The K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer (2008) Biochemistry 47, 3564-3575
  T. Heitkamp, R. Kalinowski, B. Böttcher, M. Börsch, K. Altendorf, J.-C. Greie
  
• The proton-translocating a subunit of FoF1-ATP synthase is allocated asymmetrically to the peripheral stalk (2008) J. Biol. Chem. 283, 33602-33610
  M. G. Düser, Y. Bi, N. Zarrabi, S.D. Dunn, M. Börsch
  
• Mechanistic basis for differential inhibition of the F1Fo-ATPase by Aurovertin (2009) Biopolymers 91, 830-840
  K. M. Johnson, L. Swenson, A, W. Opipari, R. Reuter, N. Zarrabi, C. A. Fierke, M. Börsch, G. D. Glick
  
• Poly(BODIPY)s: a new class of tunable polymeric dyes (2009) Macromolecules 42, 6529-6536
  F. E. Alemdaroglu, S. C. Alexander, D. Ji, D. K. Prusty, M. Börsch, A. Herrmann