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Literature DB >> 12624914

Single-molecule imaging of rotation of F1-ATPase.

Kengo Adachi¹, Hiroyuki Noji, Kazuhiko Kinosita.

Abstract

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Year: 2003 PMID： 12624914 DOI： 10.1016/s0076-6879(03)61013-x

Source DB: PubMed Journal: Methods Enzymol ISSN： 0076-6879 Impact factor: 1.600

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10 in total

1. One rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolar.

Authors: Naoyoshi Sakaki; Rieko Shimo-Kon; Kengo Adachi; Hiroyasu Itoh; Shou Furuike; Eiro Muneyuki; Masasuke Yoshida; Kazuhiko Kinosita
Journal: Biophys J Date: 2004-12-30 Impact factor: 4.033

2. The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.

Authors: Mohammad Delawar Hossain; Shou Furuike; Yasushi Maki; Kengo Adachi; M Yusuf Ali; Mominul Huq; Hiroyasu Itoh; Masasuke Yoshida; Kazuhiko Kinosita
Journal: Biophys J Date: 2006-06-01 Impact factor: 4.033

3. Torque generation in F1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice.

Authors: Ayako Kohori; Ryohei Chiwata; Mohammad Delawar Hossain; Shou Furuike; Katsuyuki Shiroguchi; Kengo Adachi; Masasuke Yoshida; Kazuhiko Kinosita
Journal: Biophys J Date: 2011-07-06 Impact factor: 4.033

4. Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites.

Authors: Nelli Mnatsakanyan; Yunxiang Li; Joachim Weber
Journal: J Biol Chem Date: 2018-12-03 Impact factor: 5.157

Single-molecule imaging of rotation of F1-ATPase.

1. One rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolar.

2. The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.

3. Torque generation in F1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice.

4. Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites.

5. The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length.

6. Calmodulin, conformational states, and calcium signaling. A single-molecule perspective.

7. Neither helix in the coiled coil region of the axle of F1-ATPase plays a significant role in torque production.

8. Role of the DELSEED loop in torque transmission of F1-ATPase.

9. Temperature dependence of the rotation and hydrolysis activities of F1-ATPase.

10. None of the rotor residues of F1-ATPase are essential for torque generation.