Literature DB >> 2882655

The loose coupling mechanism in molecular machines of living cells.

F Oosawa, S Hayashi.   

Abstract

For a bacterial flagellar motor driven by a proton flux, a loose coupling mechanism has been proposed in which the movement of the proton is indirectly and loosely coupled with the rotation of the motor. This mechanism assures the efficient and smooth conversion of both electrical and chemical potential energies of the proton of the same order as the energy of the thermal fluctuation. Loose coupling has been also assumed for the proton ATPase. A proton flux produces a rotational movement of protein molecules and this movement promotes the synthesis of ATP. In the proposed mechanism, the number of protons necessary for the synthesis of one ATP molecule is not an integer but varies depending on the environmental condition. In the case of muscle, the coupling between the hydrolysis of ATP and the shortening was found to be extremely loose. It is likely that molecular machines in living cells often adopt a loose coupling mechanism in which the chemical reaction and the physical cycle have not always a definite one-to-one correspondence.

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Year:  1986        PMID: 2882655     DOI: 10.1016/0065-227x(86)90005-5

Source DB:  PubMed          Journal:  Adv Biophys        ISSN: 0065-227X


  30 in total

Review 1.  Theories of rotary motors.

Authors:  R M Berry
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

Review 2.  A rotary molecular motor that can work at near 100% efficiency.

Authors:  K Kinosita; R Yasuda; H Noji; K Adachi
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

3.  Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging.

Authors:  K Adachi; R Yasuda; H Noji; H Itoh; Y Harada; M Yoshida; K Kinosita
Journal:  Proc Natl Acad Sci U S A       Date:  2000-06-20       Impact factor: 11.205

4.  The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer.

Authors:  Ryohei Yasuda; Tomoko Masaike; Kengo Adachi; Hiroyuki Noji; Hiroyasu Itoh; Kazuhiko Kinosita
Journal:  Proc Natl Acad Sci U S A       Date:  2003-07-22       Impact factor: 11.205

Review 5.  Myosin step size: estimates from motility assays and shortening muscle.

Authors:  K Burton
Journal:  J Muscle Res Cell Motil       Date:  1992-12       Impact factor: 2.698

6.  Chemo-mechanical coupling in F(1)-ATPase revealed by catalytic site occupancy during catalysis.

Authors:  Rieko Shimo-Kon; Eiro Muneyuki; Hiroshi Sakai; Kengo Adachi; Masasuke Yoshida; Kazuhiko Kinosita
Journal:  Biophys J       Date:  2010-04-07       Impact factor: 4.033

7.  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

8.  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

9.  Co-evolutionary analysis of domains in interacting proteins reveals insights into domain-domain interactions mediating protein-protein interactions.

Authors:  Raja Jothi; Praveen F Cherukuri; Asba Tasneem; Teresa M Przytycka
Journal:  J Mol Biol       Date:  2006-08-01       Impact factor: 5.469

10.  Mechanism and kinetics of a sodium-driven bacterial flagellar motor.

Authors:  Chien-Jung Lo; Yoshiyuki Sowa; Teuta Pilizota; Richard M Berry
Journal:  Proc Natl Acad Sci U S A       Date:  2013-06-20       Impact factor: 11.205

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