2.11 Inconsistency of Prevailing View with Some of Recent Experimental Facts
27
detachment of myosin from F-actin [52, 53]. However, this conclusion is not correct.
First, such an input is not necessitated for any elementary process in the unidirectional
movement. Second, the detachment stems from the structural change of myosin upon
the ATP binding followed by the aforementioned change in Φ F-actin (y).
References
1. Kodama T (2018) Energetics of Myosin ATP hydrolysis by calorimetry. In: Suzuki M (ed)
The role of water in ATP hydrolysis energy transduction by protein machinery, Chapter 7, Part
II, Springer Briefs in Molecular Science, Springer, ISBN: 978-981-10-8458-4, pp 103–111
(2018)
2. Kodama T (1985) Physiol Rev 65:467
3. Alberty RA (1994) Pure Appl Chem 66:1641
4. Voet D, Voet JG (2004) Biochemistry, 3rd edn. Wiley, New York
5. Kitamura K, Tokunaga M, Iwane AH, Yanagida T (1999) Nature 397:129
6. Kitamura K, Tokunaga M, Esaki S, Iwane AH, Yanagida T (2005) Biophysics 1:1
7. Ward A, Reyes CL, Yu J, Roth CB, Chang G (2007) Proc Natl Acad Sci USA 104:19005
8. Hollenstein K, Dawson RJP, Locher KP (2007) Curr Opin Struct Biol 17:412
9. Shimabukuro K, Yasuda R, Muneyuki E, Hara KY, Kinosita K Jr, Yoshida M (2003) Proc Natl
Acad Sci USA 100:14731
10. Adachi K, Oiwa K, Nishizaka T, Furuike S, Noji H, Itoh H, Yoshida M, Kinosita K Jr (2007)
Cell 130:309
11. Kinoshita M (2002) J Chem Phys 116:3493
12. Kinoshita M (2006) Chem Eng Sci 61:2150
13. Kinoshita M (2004) Chem Phys Lett 387:54
14. Kinoshita M (2016) Mechanism of functional expression of the molecular machines. Springer
Briefs in Molecular Science, Springer, ISBN: 978-981-10-1484-0
15. Kinoshita M (2013) Biophys Rev 5:283
16. Soda K (1993) J Phys Soc Jpn 62:1782
17. Asakura S, Oosawa F (1954) J Chem Phys 22:1255
18. Asakura S, Oosawa F (1958) J Polym Sci 33:183
19. Hansen J-P, McDonald LR (2006) Theory of simple liquids, 3rd edn. Academic Press, London
20. Kinoshita M, Hayashi T (2017) Phys Chem Chem Phys 19:25891
21. Kinoshita M (unpublished results)
22. Hikiri S, Hayashi T, Inoue M, Ekimoto T, Ikeguchi M, Kinoshita M (2019) J Chem Phys
150:175101
23. Hayashi T, Matsuda T, Nagata T, Katahira M, Kinoshita M (2018) Phys Chem Chem Phys
20:9167
24. Yamada T, Hayashi T, Hikiri S, Kobayashi N, Yanagida H, Ikeguchi M, Katahira M, Nagata T,
Kinoshita M (2019) J Chem Inf Model 59:3533
25. Kinoshita M, Harano Y (2005) Bull Chem Soc Jpn 78:1431
26. Hayashi T, Oshima H, Mashima T, Nagata T, Katahira M, Kinoshita M (2014) Nucleic Acids
Res 42:6861
27. Hikiri S, Yoshidome T, Ikeguchi M (2016) J Chem Theory Comput 12:5990
28. Yasuda S, Yoshidome T, Oshima H, Kodama R, Harano Y, Kinoshita M (2010) J. Chem. Phys.
132:065105
29. Yasuda S, Oshima H, Kinoshita M (2012) J Chem Phys 137:135103
30. Hayashi T, Yasuda S, Škrbi´ c T, Giacometti A, Kinoshita M (2017) J Chem Phys 147:125102
31. Hayashi T, Inoue M, Yasuda S, Petretto E, Škrbi´ c T, Giacometti A, Kinoshita M (2018) J Chem
Phys 149:045105
27
detachment of myosin from F-actin [52, 53]. However, this conclusion is not correct.
First, such an input is not necessitated for any elementary process in the unidirectional
movement. Second, the detachment stems from the structural change of myosin upon
the ATP binding followed by the aforementioned change in Φ F-actin (y).
References
1. Kodama T (2018) Energetics of Myosin ATP hydrolysis by calorimetry. In: Suzuki M (ed)
The role of water in ATP hydrolysis energy transduction by protein machinery, Chapter 7, Part
II, Springer Briefs in Molecular Science, Springer, ISBN: 978-981-10-8458-4, pp 103–111
(2018)
2. Kodama T (1985) Physiol Rev 65:467
3. Alberty RA (1994) Pure Appl Chem 66:1641
4. Voet D, Voet JG (2004) Biochemistry, 3rd edn. Wiley, New York
5. Kitamura K, Tokunaga M, Iwane AH, Yanagida T (1999) Nature 397:129
6. Kitamura K, Tokunaga M, Esaki S, Iwane AH, Yanagida T (2005) Biophysics 1:1
7. Ward A, Reyes CL, Yu J, Roth CB, Chang G (2007) Proc Natl Acad Sci USA 104:19005
8. Hollenstein K, Dawson RJP, Locher KP (2007) Curr Opin Struct Biol 17:412
9. Shimabukuro K, Yasuda R, Muneyuki E, Hara KY, Kinosita K Jr, Yoshida M (2003) Proc Natl
Acad Sci USA 100:14731
10. Adachi K, Oiwa K, Nishizaka T, Furuike S, Noji H, Itoh H, Yoshida M, Kinosita K Jr (2007)
Cell 130:309
11. Kinoshita M (2002) J Chem Phys 116:3493
12. Kinoshita M (2006) Chem Eng Sci 61:2150
13. Kinoshita M (2004) Chem Phys Lett 387:54
14. Kinoshita M (2016) Mechanism of functional expression of the molecular machines. Springer
Briefs in Molecular Science, Springer, ISBN: 978-981-10-1484-0
15. Kinoshita M (2013) Biophys Rev 5:283
16. Soda K (1993) J Phys Soc Jpn 62:1782
17. Asakura S, Oosawa F (1954) J Chem Phys 22:1255
18. Asakura S, Oosawa F (1958) J Polym Sci 33:183
19. Hansen J-P, McDonald LR (2006) Theory of simple liquids, 3rd edn. Academic Press, London
20. Kinoshita M, Hayashi T (2017) Phys Chem Chem Phys 19:25891
21. Kinoshita M (unpublished results)
22. Hikiri S, Hayashi T, Inoue M, Ekimoto T, Ikeguchi M, Kinoshita M (2019) J Chem Phys
150:175101
23. Hayashi T, Matsuda T, Nagata T, Katahira M, Kinoshita M (2018) Phys Chem Chem Phys
20:9167
24. Yamada T, Hayashi T, Hikiri S, Kobayashi N, Yanagida H, Ikeguchi M, Katahira M, Nagata T,
Kinoshita M (2019) J Chem Inf Model 59:3533
25. Kinoshita M, Harano Y (2005) Bull Chem Soc Jpn 78:1431
26. Hayashi T, Oshima H, Mashima T, Nagata T, Katahira M, Kinoshita M (2014) Nucleic Acids
Res 42:6861
27. Hikiri S, Yoshidome T, Ikeguchi M (2016) J Chem Theory Comput 12:5990
28. Yasuda S, Yoshidome T, Oshima H, Kodama R, Harano Y, Kinoshita M (2010) J. Chem. Phys.
132:065105
29. Yasuda S, Oshima H, Kinoshita M (2012) J Chem Phys 137:135103
30. Hayashi T, Yasuda S, Škrbi´ c T, Giacometti A, Kinoshita M (2017) J Chem Phys 147:125102
31. Hayashi T, Inoue M, Yasuda S, Petretto E, Škrbi´ c T, Giacometti A, Kinoshita M (2018) J Chem
Phys 149:045105