help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow A correction has been published
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pänke, O.
Right arrow Articles by Junge, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pänke, O.
Right arrow Articles by Junge, W.

Biophys J, September 2001, p. 1220-1233, Vol. 81, No. 3

Viscoelastic Dynamics of Actin Filaments Coupled to Rotary F-ATPase: Angular Torque Profile of the Enzyme

Oliver Pänke, Dmitry A. Cherepanov, Karin Gumbiowski, Siegfried Engelbrecht, and Wolfgang Junge

Division of Biophysics, University of Osnabrück, D-49069 Osnabrück, Germany

ATP synthase (FOF1) operates as two rotary motor/generators coupled by a common shaft. Both portions, F1 and FO, are rotary steppers. Their symmetries are mismatched (C3 versus C10-14). We used the curvature of fluorescent actin filaments, attached to the rotating c-ring, as a spring balance (flexural rigidity of 8 · 10-26 Nm2) to gauge the angular profile of the output torque at FO during ATP hydrolysis by F1 (see theoretical companion article (Cherepanov, D. A., and W. Junge, 2001. Biophys. J. 81:1234-1244.)). The large average output torque (50 ± 6 pN · nm) proved the absence of any slip. Variations of the torque were small, and the output free energy of the loaded enzyme decayed almost linearly over the angular reaction coordinate. Considering the threefold stepping and high activation barrier of the driving motor proper, the rather constant output torque implied a soft elastic power transmission between F1 and FO. It is considered as essential, not only for the robust operation of this ubiquitous enzyme under symmetry mismatch, but also for a high turnover rate of the two counteracting and stepping motor/generators.

Biophys J, September 2001, p. 1220-1233, Vol. 81, No. 3
© 2001 by the Biophysical Society   0006-3495/01/09/1220/14  $2.00



This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
H. Sielaff, H. Rennekamp, A. Wachter, H. Xie, F. Hilbers, K. Feldbauer, S. D. Dunn, S. Engelbrecht, and W. Junge
Domain compliance and elastic power transmission in rotary FOF1-ATPase
PNAS, November 18, 2008; 105(46): 17760 - 17765.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
H. Sielaff, H. Rennekamp, S. Engelbrecht, and W. Junge
Functional Halt Positions of Rotary FOF1-ATPase Correlated with Crystal Structures
Biophys. J., November 15, 2008; 95(10): 4979 - 4987.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
M. D. Hossain, S. Furuike, Y. Maki, K. Adachi, T. Suzuki, A. Kohori, H. Itoh, M. Yoshida, and K. Kinosita Jr.
Neither Helix in the Coiled Coil Region of the Axle of F1-ATPase Plays a Significant Role in Torque Production
Biophys. J., November 15, 2008; 95(10): 4837 - 4844.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
E. Muneyuki, T. Watanabe-Nakayama, T. Suzuki, M. Yoshida, T. Nishizaka, and H. Noji
Single Molecule Energetics of F1-ATPase Motor
Biophys. J., March 1, 2007; 92(5): 1806 - 1812.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
M. D. Hossain, S. Furuike, Y. Maki, K. Adachi, M. Y. Ali, M. Huq, H. Itoh, M. Yoshida, and K. Kinosita Jr.
The Rotor Tip Inside a Bearing of a Thermophilic F1-ATPase Is Dispensable for Torque Generation
Biophys. J., June 1, 2006; 90(11): 4195 - 4203.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Krebstakies, B. Zimmermann, P. Graber, K. Altendorf, M. Borsch, and J.-C. Greie
Both Rotor and Stator Subunits Are Necessary for Efficient Binding of F1 to F0 in Functionally Assembled Escherichia coli ATP Synthase
J. Biol. Chem., September 30, 2005; 280(39): 33338 - 33345.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
N. Sakaki, R. Shimo-Kon, K. Adachi, H. Itoh, S. Furuike, E. Muneyuki, M. Yoshida, and K. Kinosita Jr.
One Rotary Mechanism for F1-ATPase over ATP Concentrations from Millimolar down to Nanomolar
Biophys. J., March 1, 2005; 88(3): 2047 - 2056.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
B. A. Feniouk, M. A. Kozlova, D. A. Knorre, D. A. Cherepanov, A. Y. Mulkidjanian, and W. Junge
The Proton-Driven Rotor of ATP Synthase: Ohmic Conductance (10 fS), and Absence of Voltage Gating
Biophys. J., June 1, 2004; 86(6): 4094 - 4109.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Weber, S. Wilke-Mounts, S. Nadanaciva, and A. E. Senior
Quantitative Determination of Direct Binding of b Subunit to F1 in Escherichia coli F1F0-ATP Synthase
J. Biol. Chem., March 19, 2004; 279(12): 11253 - 11258.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
Y. Q. Gao, W. Yang, R. A. Marcus, and M. Karplus
A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F1-ATPase
PNAS, September 30, 2003; 100(20): 11339 - 11344.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Weber, S. Wilke-Mounts, and A. E. Senior
Identification of the F1-binding Surface on the delta -Subunit of ATP Synthase
J. Biol. Chem., April 4, 2003; 278(15): 13409 - 13416.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Muller, O. Panke, W. Junge, and S. Engelbrecht
F1-ATPase, the C-terminal End of Subunit gamma Is Not Required for ATP Hydrolysis-driven Rotation
J. Biol. Chem., June 21, 2002; 277(26): 23308 - 23313.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Gumbiowski, D. Cherepanov, M. Muller, O. Panke, P. Promto, S. Winkler, W. Junge, and S. Engelbrecht
F-ATPase: Forced Full Rotation of the Rotor Despite Covalent Cross-link with the Stator
J. Biol. Chem., November 2, 2001; 276(45): 42287 - 42292.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2001 by the Biophysical Society.