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

Kinosita, Kazuhiko; Yasuda, Ryohei; Noji, Hiroyuki; Adachi, K.

doi:10.1098/rstb.2000.0589

Cited by 226 publications

(155 citation statements)

References 68 publications

(131 reference statements)

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“…The steadystate ATPase activity, at 2 mM ATP, of Cy3-F1 attached to the Ni-NTA glass surface was 19 s Ϫ1 and was Ϸ30% of that in solution, suggesting that Ϸ70% was denatured on the surface. The initial activity in solution at 2 mM ATP was 239 s Ϫ1 , which decreased to the steady-state level of 67 s Ϫ1 because of the MgADP inhibition (28). These numbers imply that Ͻ10% of the F1 molecules on the surface are expected to be active.…”

Section: Resultsmentioning

confidence: 99%

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Stepping rotation of F ₁ -ATPase visualized through angle-resolved single-fluorophore imaging

Adachi

Yasuda

Noji

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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211

167

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Orientation dependence of single-fluorophore intensity was exploited in order to videotape conformational changes in a protein machine in real time. The fluorophore Cy3 attached to the central subunit of F 1-ATPase revealed that the subunit rotates in the molecule in discrete 120°steps and that each step is driven by the hydrolysis of one ATP molecule. These results, unlike those from the previous study under a frictional load, show that the 120°s tepping is a genuine property of this molecular motor. The data also show that the rate of ATP binding is insensitive to the load exerted on the rotor subunit.

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Section: Resultsmentioning

confidence: 99%

“…stepping rates were estimated on the most active F 1 in the sample. A likely cause is MgADP inhibition (28), which may also be responsible for the dip in hydrolysis rate around 10 1 to 10 2 M ATP (Fig. 4 Inset).…”

Section: Resultsmentioning

confidence: 99%

Stepping rotation of F ₁ -ATPase visualized through angle-resolved single-fluorophore imaging

Adachi

Yasuda

Noji

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

211

167

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“…These small nanosized devices can be seen in many areas of biological science [3][4][5][6][7][8]. The fluctuations present in the surrounding environment can disturb the deterministic nature of such small-scale devices.…”

Section: Introductionmentioning

confidence: 99%

Stochastic efficiency of an isothermal work-to-work converter engine

Gupta

Sabhapandit

2017

Phys. Rev. E

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We investigate the efficiency of an isothermal Brownian work-to-work converter engine, composed of a Brownian particle coupled to a heat bath at a constant temperature. The system is maintained out of equilibrium by using two external time-dependent stochastic Gaussian forces, where one is called load force and the other is called drive force. Work done by these two forces are stochastic quantities. The efficiency of this small engine is defined as the ratio of stochastic work done against load force to stochastic work done by the drive force. The probability density function as well as large deviation function of the stochastic efficiency are studied analytically and verified by numerical simulations.

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“…Thus stall is not an equilibrium state, as observed with F1 ATPase (29,30), and the backward steps that are observed at high load with kinesin (31,32) are not due to simple reversal of the forward reaction.…”

Section: Methodsmentioning

confidence: 96%

The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP

Hackney

2005

Proc. Natl. Acad. Sci. U.S.A.

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Although the steps for the forward reaction of ATP hydrolysis by the motor protein kinesin have been studied extensively, the rates for the reverse reactions and thus the energy changes at each step are not as well defined. Oxygen isotopic exchange between water and P i was used to evaluate the reverse rates. The fraction of the kinesin⅐ADP⅐P i complex that reverts to ATP before release of Pi during net hydrolysis was Ϸ0 and Ϸ2.6% in the absence and presence of microtubules (MTs), respectively. The rate of synthesis of bound ATP from free P i and the MT⅐kinesin⅐ADP complex was Ϸ1.7 M ؊1 ⅐s ؊1 (K0.5 ADP ‫؍‬ 70 M) with monomeric kinesin in the absence of net hydrolysis. Synthesis of bound ATP from the ADP of the tethered head of a dimer-MT complex was 20-fold faster than for the monomer-MT complex. This MT-activated ATP synthesis at the tethered head is in marked contrast to the lack of MT stimulation of ADP release from the same site. The more rapid ATP synthesis with dimers suggests that the tethered head binds behind the strongly attached head, because this positions the neck linker of the tethered head toward the plus end of the MT and would thus facilitate its docking on synthesis of ATP. The observed rate of ATP synthesis also puts limits on the overall energetics that suggest that a significant fraction of the free energy of ATP hydrolysis is available to drive the docking of the neck linker on binding of ATP.ATPase ͉ energy coupling ͉ motility ͉ motor protein ͉ isotopic exchange K inesin-1 is molecular motor that moves along microtubules (MTs) in a highly processive manner. Scheme 1 presents a minimal mechanism for ATP hydrolysis by the MT complex of a kinesin monomer motor domain (see refs. 1-3 for recent reviews of the ATPase mechanism and coupling to motility). ATP binds rapidly and is hydrolyzed at 100-300 s Ϫ1 . P i release occurs without a lag after hydrolysis, and thus P i release is at least as fast as hydrolysis (k 3 Ն k 2 ). ADP release is partially ratelimiting for conventional kinesin-1 and may be the principal rate limiting step for some other kinesin superfamily members.Another important aspect, however, is the equilibrium constant of each step, because it determines the free energy that is available at that step for coupling to movement against a load. The equilibrium constants can be determined if the rates in the reverse direction are known, but this is difficult because the overall equilibrium strongly favors hydrolysis. Oxygen isotopic exchange is a powerful technique for evaluation of the reversibility of the hydrolysis reaction and has provided important insight into the mechanism of the F1-ATPase (4) and myosin (5, 6). It is used here to determine the rates of the reverse reactions of kinesin.Hydrolysis of ATP by kinesin proceeds through attack of water on the ␥ phosphoryl to yield P i that contains one water-derived oxygen and three oxygens from the nonbridge ␥ oxygens of the ATP, as indicated in Scheme 2 for hydrolysis of unenriched ATP in 100% 18 O-enriched water. If P i release vi...

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

Cited by 226 publications

References 68 publications

Stepping rotation of F ₁ -ATPase visualized through angle-resolved single-fluorophore imaging

Stepping rotation of F ₁ -ATPase visualized through angle-resolved single-fluorophore imaging

Stochastic efficiency of an isothermal work-to-work converter engine

The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP

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

Cited by 226 publications

References 68 publications

Stepping rotation of F 1 -ATPase visualized through angle-resolved single-fluorophore imaging

Stepping rotation of F 1 -ATPase visualized through angle-resolved single-fluorophore imaging

Stochastic efficiency of an isothermal work-to-work converter engine

The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP

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Stepping rotation of F ₁ -ATPase visualized through angle-resolved single-fluorophore imaging

Stepping rotation of F ₁ -ATPase visualized through angle-resolved single-fluorophore imaging