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Nishizaka, T., Oiwa, K., Noji, H., Kimura, S., Muneyuki, E., Yoshida, M., & Kinosita, K. (2004). Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation. Nature Structural & Molecular Biology, 11(2), 142–148.

Authors 7
  1. Takayuki Nishizaka (first)
  2. Kazuhiro Oiwa (additional)
  3. Hiroyuki Noji (additional)
  4. Shigeki Kimura (additional)
  5. Eiro Muneyuki (additional)
  6. Masasuke Yoshida (additional)
  7. Kazuhiko Kinosita (additional)
References 35 Referenced 252
  1. Abrahams, J.P., Leslie, A.G., Lutter, R. & Walker, J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621–628 (1994). (10.1038/370621a0) / Nature by JP Abrahams (1994)
  2. Boyer, P.D. The binding change mechanism for ATP synthase—some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215–250 (1993). (10.1016/0005-2728(93)90063-L) / Biochim. Biophys. Acta by PD Boyer (1993)
  3. Boyer, P.D. The ATP synthase—a splendid molecular machine. Annu. Rev. Biochem. 66, 717–749 (1997). (10.1146/annurev.biochem.66.1.717) / Annu. Rev. Biochem. by PD Boyer (1997)
  4. Yoshida, M., Muneyuki, E. & Hisabori, T. ATP synthase—a marvelous rotary engine of the cell. Nat. Rev. Mol. Cell Biol. 2, 669–677 (2001). (10.1038/35089509) / Nat. Rev. Mol. Cell Biol. by M Yoshida (2001)
  5. Noji, H., Yasuda, R., Yoshida, M. & Kinosita, K. Jr. Direct observation of the rotation of F1-ATPase. Nature 386, 299–302 (1997). (10.1038/386299a0) / Nature by H Noji (1997)
  6. Noji, H. et al. Purine but not pyrimidine nucleotides support rotation of F1-ATPase. J. Biol. Chem. 276, 25480–25486 (2001). (10.1074/jbc.M102200200) / J. Biol. Chem. by H Noji (2001)
  7. Yasuda, R., Noji, H., Kinosita, K. Jr. & Yoshida, M. F1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell 93, 1117–1124 (1998). (10.1016/S0092-8674(00)81456-7) / Cell by R Yasuda (1998)
  8. Adachi, K. et al. Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging. Proc. Natl. Acad. Sci. USA 97, 7243–7247 (2000). (10.1073/pnas.120174297) / Proc. Natl. Acad. Sci. USA by K Adachi (2000)
  9. Boyer, P.D. Catalytic site forms and controls in ATP synthase catalysis. Biochim. Biophys. Acta 1458, 252–262 (2000). (10.1016/S0005-2728(00)00077-3) / Biochim. Biophys. Acta by PD Boyer (2000)
  10. Kinosita, K. Jr., Yasuda, R., Noji, H. & Adachi, K. A rotary molecular motor that can work at near 100% efficiency. Phil. Trans. R. Soc. Lond. B 355, 473–489 (2000). (10.1098/rstb.2000.0589) / Phil. Trans. R. Soc. Lond. B by K Kinosita Jr. (2000)
  11. Weber, J. & Senior, A.E. ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis. Biochim. Biophys. Acta 1458, 300–309 (2000). (10.1016/S0005-2728(00)00082-7) / Biochim. Biophys. Acta by J Weber (2000)
  12. Yasuda, R., Noji, H., Yoshida, M., Kinosita, K. Jr. & Itoh, H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 410, 898–904 (2001). (10.1038/35073513) / Nature by R Yasuda (2001)
  13. Oiwa, K. et al. Comparative single-molecule and ensemble myosin enzymology: sulfoindocyanine ATP and ADP derivatives. Biophys. J. 78, 3048–3071 (2000). (10.1016/S0006-3495(00)76843-3) / Biophys. J. by K Oiwa (2000)
  14. Tokunaga, M., Kitamura, K., Saito, K., Iwane, A.H. & Yanagida, T. Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy. Biochem. Biophys. Res. Commun. 235, 47–53 (1997). (10.1006/bbrc.1997.6732) / Biochem. Biophys. Res. Commun. by M Tokunaga (1997)
  15. Funatsu, T., Harada, Y., Tokunaga, M., Saito, K. & Yanagida, T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374, 555–559 (1995). (10.1038/374555a0) / Nature by T Funatsu (1995)
  16. Ishijima, A. et al. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161–171 (1998). (10.1016/S0092-8674(00)80911-3) / Cell by A Ishijima (1998)
  17. Ha, T., Enderle, T., Chemla, S., Selvin, R. & Weiss, S. Single molecule dynamics studied by polarization modulation. Phys. Rev. Lett. 77, 3979–3982 (1996). (10.1103/PhysRevLett.77.3979) / Phys. Rev. Lett. by T Ha (1996)
  18. Sase, I., Miyata, H., Ishiwata, S. & Kinosita, K. Jr. Axial rotation of sliding actin filaments revealed by single-fluorophore imaging. Proc. Natl. Acad. Sci. USA 94, 5646–5650 (1997). (10.1073/pnas.94.11.5646) / Proc. Natl. Acad. Sci. USA by I Sase (1997)
  19. Axelrod, D. Total internal reflection fluorescence at biological surfaces. in Noninvasive Techniques in Cell Biology (eds. Foskett, J.K. & Grinstein, S.) 93–127 (Wiley-Liss, New York, 1990). / Noninvasive Techniques in Cell Biology by D Axelrod (1990)
  20. Jault, J.M. et al. The α3β3γ subcomplex of the F1-ATPase from the thermophilic bacillus PS3 with the βT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover. J. Biol. Chem. 271, 28818–28824 (1996). (10.1074/jbc.271.46.28818) / J. Biol. Chem. by JM Jault (1996)
  21. Matsui, T. et al. Catalytic activity of the α3β3γ complex of F1-ATPase without noncatalytic nucleotide binding site. J. Biol. Chem. 272, 8215–8221 (1997). (10.1074/jbc.272.13.8215) / J. Biol. Chem. by T Matsui (1997)
  22. Hirono-Hara, Y. et al. Pause and rotation of F1-ATPase during catalysis. Proc. Natl. Acad. Sci. USA 98, 13649–13654 (2001). (10.1073/pnas.241365698) / Proc. Natl. Acad. Sci. USA by Y Hirono-Hara (2001)
  23. Vale, R.D. & Oosawa, F. Protein motors and Maxwell's demons: does mechanochemical transduction involve a thermal ratchet? Adv. Biophys. 26, 97–134 (1990). (10.1016/0065-227X(90)90009-I) / Adv. Biophys. by RD Vale (1990)
  24. Astumian, R.D. & Bier, M. Fluctuation driven ratchets: molecular motors. Phys. Rev. Lett. 72, 1766–1769 (1994). (10.1103/PhysRevLett.72.1766) / Phys. Rev. Lett. by RD Astumian (1994)
  25. Hunt, A.J., Gittes, F. & Howard, J. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67, 766–781 (1994). (10.1016/S0006-3495(94)80537-5) / Biophys. J. by AJ Hunt (1994)
  26. Masaike, T., Muneyuki, E., Noji, H., Kinosita, K. Jr. & Yoshida, M. F1-ATPase changes its conformations upon phosphate release. J. Biol. Chem. 277, 21643–21649 (2002). (10.1074/jbc.M110297200) / J. Biol. Chem. by T Masaike (2002)
  27. Shimabukuro, K. et al. Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40° substep rotation. Proc. Natl. Acad. Sci. USA 100, 14731–14736 (2003). (10.1073/pnas.2434983100) / Proc. Natl. Acad. Sci. USA by K Shimabukuro (2003)
  28. Weber, J. & Senior, A.E. Bi-site catalysis in F1-ATPase: does it exist? J. Biol. Chem. 276, 35422–35428 (2001). (10.1074/jbc.M104946200) / J. Biol. Chem. by J Weber (2001)
  29. Boyer, P.D. Catalytic site occupancy during ATP synthase catalysis. FEBS Lett. 512, 29–32 (2002). (10.1016/S0014-5793(02)02293-7) / FEBS Lett. by PD Boyer (2002)
  30. Masaike, T. et al. Rotation of F1-ATPase and the hinge residues of the β subunit. J. Exp. Biol. 203, 1–8 (2000). (10.1242/jeb.203.1.1) / J. Exp. Biol. by T Masaike (2000)
  31. Dou, C., Fortes, P.A. & Allison, W.S. The α3(βY341W)3 γ subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP. Biochemistry 37, 16757–16764 (1998). (10.1021/bi981717q) / Biochemistry by C Dou (1998)
  32. Ren, H. & Allison, W.S. Substitution of betaGlu201 in the α3β3γ subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides. J. Biol. Chem. 275, 10057–10063 (2000). (10.1074/jbc.275.14.10057) / J. Biol. Chem. by H Ren (2000)
  33. Mitome, N. et al. The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F1-ATPase. Eur. J. Biochem. 269, 53–60 (2002). (10.1046/j.0014-2956.2002.02623.x) / Eur. J. Biochem. by N Mitome (2002)
  34. Nishizaka, T., Seo, R., Tadakuma, H., Kinosita, K. Jr. & Ishiwata, S. Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties. Biophys. J. 79, 962–974 (2000). (10.1016/S0006-3495(00)76350-8) / Biophys. J. by T Nishizaka (2000)
  35. Nishizaka, T., Miyata, H., Yoshikawa, H., Ishiwata, S. & Kinosita, K. Jr. Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature 377, 251–254 (1995). (10.1038/377251a0) / Nature by T Nishizaka (1995)
Dates
Type When
Created 21 years, 7 months ago (Jan. 18, 2004, 2:38 p.m.)
Deposited 2 years, 3 months ago (May 19, 2023, 12:52 a.m.)
Indexed 2 weeks, 4 days ago (Aug. 6, 2025, 9:11 a.m.)
Issued 21 years, 7 months ago (Jan. 18, 2004)
Published 21 years, 7 months ago (Jan. 18, 2004)
Published Online 21 years, 7 months ago (Jan. 18, 2004)
Published Print 21 years, 6 months ago (Feb. 1, 2004)
Funders 0

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@article{Nishizaka_2004, title={Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation}, volume={11}, ISSN={1545-9985}, url={http://dx.doi.org/10.1038/nsmb721}, DOI={10.1038/nsmb721}, number={2}, journal={Nature Structural & Molecular Biology}, publisher={Springer Science and Business Media LLC}, author={Nishizaka, Takayuki and Oiwa, Kazuhiro and Noji, Hiroyuki and Kimura, Shigeki and Muneyuki, Eiro and Yoshida, Masasuke and Kinosita, Kazuhiko}, year={2004}, month=jan, pages={142–148} }