3.8 Inverse Rotation Compelled by External Torque Imposed …
61
It is remarkable that the thermodynamic behavior of F 1 -ATPase is substantially
influenced by the mutation E190D. However, portions closely packed like a threedimensional jigsaw puzzle can be perturbed to a drastic extent even by a single
mutation, giving rise to a significant modification of the packing structure of the
whole protein complex. This modification may be responsible for the deterioration
of the ATPase activity [36] and the lengthened catalytic dwell [24].
3.8.5 F o F 1 -ATP Synthase
F o F 1 -ATP synthase [37] synthesizes ATP in virtually all cells. F o is within the
membrane and F 1 is in the intracellular region. The γ subunit, which connects F o
and F 1 , is incorporated in both of them. F 1 -ATPase, the α 3 β 3 γ complex separated
from F o F 1 -ATP synthase, hydrolyses ATP. In F o −γ, sufficiently large W (W is an
energy given to the system; see Eq. (3.2)) is realized by the coupling with the transfer
of protons from the higher-proton-concentration (extracellular) region to the lowerproton-concentration (intracellular) region, an irreversible process accompanied by a
free-energy decrease of ~−9k B T (T = 298 K) [37]. As a result, the γ subunit rotates
in the inverse direction in F 1 with the occurrence of ATP synthesis. A transfer of
three protons is required for synthesizing one ATP molecule.
References
1. Uchihashi T, Iino R, Ando T, Noji H (2011) Science 333:755
2. Shirakihara Y, Yohda M, Kagawa Y, Yokoyama K, Yoshida M (1991) J Biochem 109:466
3. Bowler MW, Montgomery MG, Leslie AGW, Walker JE (2007) J Biol Chem 282:14238
4. Abrahams JP, Leslie AG, Lutter R, Walker JE (1994) Nature 370:621
5. Kabaleeswaran V, Shen H, Symersky J, Walker JE, Leslie AGW, Mueller DM (2009) J Biol
Chem 284:10546
6. Okuno D, Fujisawa R, Iino R, Hirono-Hara Y, Imamura H, Noji H (2008) Proc Natl Acad Sci
USA 105:20722
7. Sieladd H, Rennekamp H, Engelbrecht S, Junge W (2008) Biophys J 95:4979
8. Masaike T, Koyama-Horibe F, Oiwa K, Yoshida M, Nishizaka T (2008) Nat Struct Mol Biol
15:1326
9. Watanabe R, Iino R, Noji H (2010) Nat Chem Biol 6:814
10. Ito Y, Ikeguchi M (2010) J Comput Chem 31:2175
11. Šali A, Blundell TLJ (1993) J Mol Biol 234:779
12. Gibbons C, Montgomery MG, Leslie AGW, Walker JE (2000) Nat Struct Biol 7:1055
13. Yoshidome T, Ito Y, Ikeguchi M, Kinoshita M (2011) J Am Chem Soc 133:4030
14. Kusalik PG, Patey GN (1988) J. Chem. Phys. 88:7715
15. Kusalik PG, Patey GN (1988) Mol Phys 65:1105
16. Cann NM, Patey GN (1997) J Chem Phys 106:8165
17. Kinoshita M (2008) J Chem Phys 128:024507
18. Hayashi T, Oshima H, Harano Y, Kinoshita M (2016) J Phys: Condens Matter 28:344003
19. Roth R, Harano Y, Kinoshita M (2006) Phys Rev Lett 97:078101
20. Oshima H, Kinoshita M (2015) J Chem Phys 142:145103
61
It is remarkable that the thermodynamic behavior of F 1 -ATPase is substantially
influenced by the mutation E190D. However, portions closely packed like a threedimensional jigsaw puzzle can be perturbed to a drastic extent even by a single
mutation, giving rise to a significant modification of the packing structure of the
whole protein complex. This modification may be responsible for the deterioration
of the ATPase activity [36] and the lengthened catalytic dwell [24].
3.8.5 F o F 1 -ATP Synthase
F o F 1 -ATP synthase [37] synthesizes ATP in virtually all cells. F o is within the
membrane and F 1 is in the intracellular region. The γ subunit, which connects F o
and F 1 , is incorporated in both of them. F 1 -ATPase, the α 3 β 3 γ complex separated
from F o F 1 -ATP synthase, hydrolyses ATP. In F o −γ, sufficiently large W (W is an
energy given to the system; see Eq. (3.2)) is realized by the coupling with the transfer
of protons from the higher-proton-concentration (extracellular) region to the lowerproton-concentration (intracellular) region, an irreversible process accompanied by a
free-energy decrease of ~−9k B T (T = 298 K) [37]. As a result, the γ subunit rotates
in the inverse direction in F 1 with the occurrence of ATP synthesis. A transfer of
three protons is required for synthesizing one ATP molecule.
References
1. Uchihashi T, Iino R, Ando T, Noji H (2011) Science 333:755
2. Shirakihara Y, Yohda M, Kagawa Y, Yokoyama K, Yoshida M (1991) J Biochem 109:466
3. Bowler MW, Montgomery MG, Leslie AGW, Walker JE (2007) J Biol Chem 282:14238
4. Abrahams JP, Leslie AG, Lutter R, Walker JE (1994) Nature 370:621
5. Kabaleeswaran V, Shen H, Symersky J, Walker JE, Leslie AGW, Mueller DM (2009) J Biol
Chem 284:10546
6. Okuno D, Fujisawa R, Iino R, Hirono-Hara Y, Imamura H, Noji H (2008) Proc Natl Acad Sci
USA 105:20722
7. Sieladd H, Rennekamp H, Engelbrecht S, Junge W (2008) Biophys J 95:4979
8. Masaike T, Koyama-Horibe F, Oiwa K, Yoshida M, Nishizaka T (2008) Nat Struct Mol Biol
15:1326
9. Watanabe R, Iino R, Noji H (2010) Nat Chem Biol 6:814
10. Ito Y, Ikeguchi M (2010) J Comput Chem 31:2175
11. Šali A, Blundell TLJ (1993) J Mol Biol 234:779
12. Gibbons C, Montgomery MG, Leslie AGW, Walker JE (2000) Nat Struct Biol 7:1055
13. Yoshidome T, Ito Y, Ikeguchi M, Kinoshita M (2011) J Am Chem Soc 133:4030
14. Kusalik PG, Patey GN (1988) J. Chem. Phys. 88:7715
15. Kusalik PG, Patey GN (1988) Mol Phys 65:1105
16. Cann NM, Patey GN (1997) J Chem Phys 106:8165
17. Kinoshita M (2008) J Chem Phys 128:024507
18. Hayashi T, Oshima H, Harano Y, Kinoshita M (2016) J Phys: Condens Matter 28:344003
19. Roth R, Harano Y, Kinoshita M (2006) Phys Rev Lett 97:078101
20. Oshima H, Kinoshita M (2015) J Chem Phys 142:145103