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Literature DB >> 10836505

How Fo-ATPase generates rotary torque.

Abstract

The F-ATPases synthesize ATP using a transmembrane ionmotive force (IMF) established by the electron transport chain. This transduction involves first converting the IMF to a rotary torque in the transmembrane Fo portion. This torque is communicated from Fo to the F1 portion where the energy is used to release the newly synthesized ATP from the catalytic sites according to Boyer's binding change mechanism. Here we explain the principle by which an IMF generates this rotary torque in the Fo ion engine.

Entities: Chemical

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Year: 2000 PMID： 10836505 PMCID： PMC1692753 DOI： 10.1098/rstb.2000.0593

Source DB: PubMed Journal: Philos Trans R Soc Lond B Biol Sci ISSN： 0962-8436 Impact factor: 6.237

22 in total

1. Molecular architecture of the rotary motor in ATP synthase.

Authors: D Stock; A G Leslie; J E Walker
Journal: Science Date: 1999-11-26 Impact factor: 47.728

2. ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage.

Authors: G Kaim; P Dimroth
Journal: EMBO J Date: 1999-08-02 Impact factor: 11.598

3. Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPases.

Authors: G Kaim; U Matthey; P Dimroth
Journal: EMBO J Date: 1998-02-02 Impact factor: 11.598

Review 4. ATP synthase: an electrochemical transducer with rotatory mechanics.

Authors: W Junge; H Lill; S Engelbrecht
Journal: Trends Biochem Sci Date: 1997-11 Impact factor: 13.807

5. Energy transduction in ATP synthase.

Authors: T Elston; H Wang; G Oster
Journal: Nature Date: 1998-01-29 Impact factor: 49.962

6. Cellular motions and thermal fluctuations: the Brownian ratchet.

Authors: C S Peskin; G M Odell; G F Oster
Journal: Biophys J Date: 1993-07 Impact factor: 4.033

7. Vacuolar H(+)-pumping ATPase variable transport coupling ratio controlled by pH.

Authors: J M Davies; I Hunt; D Sanders
Journal: Proc Natl Acad Sci U S A Date: 1994-08-30 Impact factor: 11.205

8. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

Authors: J P Abrahams; A G Leslie; R Lutter; J E Walker
Journal: Nature Date: 1994-08-25 Impact factor: 49.962

9. A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit.

Authors: S B Vik; B J Antonio
Journal: J Biol Chem Date: 1994-12-02 Impact factor: 5.157

10. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.

Authors: M E Girvin; V K Rastogi; F Abildgaard; J L Markley; R H Fillingame
Journal: Biochemistry Date: 1998-06-23 Impact factor: 3.162

10 in total

Review 1. Stoichiometry of energy coupling by proton-translocating ATPases: a history of variability.

Authors: J J Tomashek; W S Brusilow
Journal: J Bioenerg Biomembr Date: 2000-10 Impact factor: 2.945

2. Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.

Authors: Robert Ishmukhametov; Tassilo Hornung; David Spetzler; Wayne D Frasch
Journal: EMBO J Date: 2010-10-29 Impact factor: 11.598

3. Effects of oscillatory electric fields on internal membranes: an analytical model.

Authors: Vijayanand Vajrala; James R Claycomb; Hugo Sanabria; John H Miller
Journal: Biophys J Date: 2007-12-07 Impact factor: 4.033

4. Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.

Authors: James Martin; Jennifer Hudson; Tassilo Hornung; Wayne D Frasch
Journal: J Biol Chem Date: 2015-02-24 Impact factor: 5.157

5. Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes.

Authors: Justin York; David Spetzler; Tassilo Hornung; Robert Ishmukhametov; James Martin; Wayne D Frasch
Journal: J Bioenerg Biomembr Date: 2007-12 Impact factor: 2.945

How Fo-ATPase generates rotary torque.

1. Molecular architecture of the rotary motor in ATP synthase.

2. ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage.

3. Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPases.

Review 4. ATP synthase: an electrochemical transducer with rotatory mechanics.

5. Energy transduction in ATP synthase.

6. Cellular motions and thermal fluctuations: the Brownian ratchet.

7. Vacuolar H(+)-pumping ATPase variable transport coupling ratio controlled by pH.

8. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

9. A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit.

10. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.

Review 1. Stoichiometry of energy coupling by proton-translocating ATPases: a history of variability.

2. Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.

3. Effects of oscillatory electric fields on internal membranes: an analytical model.

4. Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.

5. Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes.

Review 6. Catalytic robustness and torque generation of the F₁-ATPase.

7. pH-dependent 11° F₁F_O ATP synthase sub-steps reveal insight into the F_O torque generating mechanism.

8. The Phylogenetic Signature Underlying ATP Synthase c-Ring Compliance.

9. Electric field driven torque in ATP synthase.

10. ATP synthase: Evolution, energetics, and membrane interactions.

Review 4. ATP synthase: an electrochemical transducer with rotatory mechanics.

Review 1. Stoichiometry of energy coupling by proton-translocating ATPases: a history of variability.

Review 6. Catalytic robustness and torque generation of the F1-ATPase.

Review 6. Catalytic robustness and torque generation of the F₁-ATPase.