抄録
F1-ATPase, a water-soluble portion of ATP synthase, is a fully reversible rotary molecular machine in which a central γ subunit rotates inside a cylinder made of three α and three β subunits alternately arranged. This motor rotates counterclockwise by hydrolyzing ATP in three catalytic sites but synthesizes ATP when forced to rotate clockwise by an external force. Single-molecule studies have revealed how the chemical reactions that occur in the three catalytic sites are coupled to mechanical rotation.
| 元の言語 | English |
|---|---|
| ホスト出版物のタイトル | Comprehensive Biophysics |
| 出版者 | Elsevier Inc. |
| ページ | 35-49 |
| ページ数 | 15 |
| 巻 | 8 |
| ISBN（印刷物） | 9780080957180 |
| DOI | |
| 出版物ステータス | Published - 2012 |
| 外部発表 | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
これを引用
Rotational catalysis by F1-ATPase. / Adachi, K.; Nishizaka, T.; Kinosita, K.
Comprehensive Biophysics. 巻 8 Elsevier Inc., 2012. p. 35-49.研究成果: Chapter
}
TY - CHAP
T1 - Rotational catalysis by F1-ATPase
AU - Adachi, K.
AU - Nishizaka, T.
AU - Kinosita, K.
PY - 2012
Y1 - 2012
N2 - F1-ATPase, a water-soluble portion of ATP synthase, is a fully reversible rotary molecular machine in which a central γ subunit rotates inside a cylinder made of three α and three β subunits alternately arranged. This motor rotates counterclockwise by hydrolyzing ATP in three catalytic sites but synthesizes ATP when forced to rotate clockwise by an external force. Single-molecule studies have revealed how the chemical reactions that occur in the three catalytic sites are coupled to mechanical rotation.
AB - F1-ATPase, a water-soluble portion of ATP synthase, is a fully reversible rotary molecular machine in which a central γ subunit rotates inside a cylinder made of three α and three β subunits alternately arranged. This motor rotates counterclockwise by hydrolyzing ATP in three catalytic sites but synthesizes ATP when forced to rotate clockwise by an external force. Single-molecule studies have revealed how the chemical reactions that occur in the three catalytic sites are coupled to mechanical rotation.
KW - ATP synthase
KW - Chemo-mechanical coupling
KW - Conformational change
KW - F-ATPase
KW - Fluorescent ATP analog
KW - Free energy
KW - High efficiency
KW - High-speed imaging
KW - Induced fit
KW - Molecular motor
KW - Power stroke
KW - Single fluorophore imaging
KW - Single-molecule study
KW - Torque generation
UR - http://www.scopus.com/inward/record.url?scp=84882803042&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84882803042&partnerID=8YFLogxK
U2 - 10.1016/B978-0-12-374920-8.00804-3
DO - 10.1016/B978-0-12-374920-8.00804-3
M3 - Chapter
AN - SCOPUS:84882803042
SN - 9780080957180
VL - 8
SP - 35
EP - 49
BT - Comprehensive Biophysics
PB - Elsevier Inc.
ER -