Abstract
F1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylinder made of α3β 3 subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting γ angle defined as 0°, phosphate is released at -200°, and ADP is released during quick rotation between 240° and 320° that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly.
| Original language | English |
|---|---|
| Pages (from-to) | 1227-1236 |
| Number of pages | 10 |
| Journal | Biophysical Journal |
| Volume | 98 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2010 Apr 7 |
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ASJC Scopus subject areas
- Biophysics
Cite this
Chemo-mechanical coupling in F1-ATPaSe revealed by catalytic site occupancy during catalysis. / Shimo-Kon, Rieko; Muneyuki, Eiro; Sakai, Hiroshi; Adachi, Kengo; Yoshida, Masasuke; Kinosita, Kazuhiko.
In: Biophysical Journal, Vol. 98, No. 7, 07.04.2010, p. 1227-1236.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Chemo-mechanical coupling in F1-ATPaSe revealed by catalytic site occupancy during catalysis
AU - Shimo-Kon, Rieko
AU - Muneyuki, Eiro
AU - Sakai, Hiroshi
AU - Adachi, Kengo
AU - Yoshida, Masasuke
AU - Kinosita, Kazuhiko
PY - 2010/4/7
Y1 - 2010/4/7
N2 - F1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylinder made of α3β 3 subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting γ angle defined as 0°, phosphate is released at -200°, and ADP is released during quick rotation between 240° and 320° that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly.
AB - F1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylinder made of α3β 3 subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting γ angle defined as 0°, phosphate is released at -200°, and ADP is released during quick rotation between 240° and 320° that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly.
UR - http://www.scopus.com/inward/record.url?scp=77950599731&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77950599731&partnerID=8YFLogxK
U2 - 10.1016/j.bpj.2009.11.050
DO - 10.1016/j.bpj.2009.11.050
M3 - Article
C2 - 20371322
AN - SCOPUS:77950599731
VL - 98
SP - 1227
EP - 1236
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 7
ER -