Literature DB >> 10838043

The rotary binding change mechanism of ATP synthases.

R L Cross1.   

Abstract

The F(0)F(1) ATP synthase functions as a rotary motor where subunit rotation driven by a current of protons flowing through F(0) drives the binding changes in F(1) that are required for net ATP synthesis. Recent work that has led to the identification of components of the rotor and stator is reviewed. In addition, a model is proposed to describe the transmission of energy from four proton transport steps to the synthesis of one ATP. Finally, some of the requirements for efficient energy coupling by a rotary binding change mechanism are considered.

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Year:  2000        PMID： 10838043     DOI： 10.1016/s0005-2728(00)00079-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  20 in total

1.  Pause and rotation of F(1)-ATPase during catalysis.

Authors:  Y Hirono-Hara; H Noji; M Nishiura; E Muneyuki; K Y Hara; R Yasuda; K Kinosita; M Yoshida
Journal:  Proc Natl Acad Sci U S A       Date:  2001-11-13       Impact factor: 11.205

Review 2.  Structural changes during ATP hydrolysis activity of the ATP synthase from Escherichia coli as revealed by fluorescent probes.

Authors:  P Turina
Journal:  J Bioenerg Biomembr       Date:  2000-08       Impact factor: 2.945

3.  Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase.

Authors:  M L Hutcheon; T M Duncan; H Ngai; R L Cross
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-03       Impact factor: 11.205

Review 4.  Assembly and regulation of the yeast vacuolar H+-ATPase.

Authors:  Patricia M Kane; Anne M Smardon
Journal:  J Bioenerg Biomembr       Date:  2003-08       Impact factor: 2.945

Review 5.  Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases.

Authors:  Takao Inoue; Stephan Wilkens; Michael Forgac
Journal:  J Bioenerg Biomembr       Date:  2003-08       Impact factor: 2.945

6.  Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane.

Authors:  Eva-Maria E Uhlemann; Hannah E Pierson; Robert H Fillingame; Oleg Y Dmitriev
Journal:  Protein Sci       Date:  2012-01-04       Impact factor: 6.725

7.  Mechanical modulation of catalytic power on F1-ATPase.

Authors:  Rikiya Watanabe; Daichi Okuno; Shouichi Sakakihara; Katsuya Shimabukuro; Ryota Iino; Masasuke Yoshida; Hiroyuki Noji
Journal:  Nat Chem Biol       Date:  2011-11-20       Impact factor: 15.040

8.  Activation of pausing F1 motor by external force.

Authors:  Yoko Hirono-Hara; Koji Ishizuka; Kazuhiko Kinosita; Masasuke Yoshida; Hiroyuki Noji
Journal:  Proc Natl Acad Sci U S A       Date:  2005-03-09       Impact factor: 11.205

9.  Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites.

Authors:  Yakov M Milgrom; Richard L Cross
Journal:  Proc Natl Acad Sci U S A       Date:  2005-09-19       Impact factor: 11.205

10.  Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation.

Authors:  Daichi Okuno; Ryo Fujisawa; Ryota Iino; Yoko Hirono-Hara; Hiromi Imamura; Hiroyuki Noji
Journal:  Proc Natl Acad Sci U S A       Date:  2008-12-15       Impact factor: 11.205
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