A model of stepping kinetics for rotary enzymes. Application to the F1-ATPase

Goldstein, B.N.; Aksirov, A. M.; Zakrjevskaya, D.T.

doi:10.1016/j.biosystems.2010.12.007

Cited by 3 publications

(2 citation statements)

References 31 publications

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“…Meanwhile, the catalytic power of F 1 -ATPpase is detailed analyzed in [15], the structure and organization of the yeast F 0 F 1 -ATP synthase are studied in [16], and the Na + , K + -ATPase in liposomal membrane are discussed in [17]. Finally, more theoretical studies can also be found in [18][19][20][21][22][23][24][25][26][27][28][29][30][31][32] for F 0 -ATPase or F 1 -ATPase, and in [33][34][35][36][37][38][39][40][41] for transmembrane motion of ions.…”

Section: Introductionmentioning

confidence: 99%

Properties of sodium-driven bacterial flagellar motor: A two-state model approach

Zhang

2015

Mod. Phys. Lett. B

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Bacterial flagellar motor (BFM) is one of the ion-driven molecular machines, which drives the rotation of flagellar filaments and enable bacteria to swim in viscous solutions. Understanding its mechanism is one challenge in biophysics. Based on previous models and inspired by the idea used in description of motor proteins, in this study one two-state model is provided. Meanwhile, according to corresponding experimental data, mathematical relationship between BFM membrane voltage and pH value of the environment, and relationship between internal and external sodium concentrations are given. Therefore, with model parameter values obtained by fitting theoretical results of torque-speed relation to recent experimental data, many biophysical properties of bacterial flagellar motor can be obtained for any pH values and any external sodium concentrations. Including the rotation speed, stall torque (i.e. the torque generated by BFM), rotation dispersion, and rotation randomness. In this study, the single-stator BFM will be firstly analyzed, and then properties of multiple-stator BFM are addressed briefly. Author SummaryBased on previous models for BFM and the idea used in the modeling of motor protein kinesin, one two-state model is present to discuss biophysical properties of BFM. From this model torque-speed relationship, dispersion and randomness of single-stator BFM can be obtained for any pH values and any external sodium concentrations. Meanwhile properties of BFM with multiple stators are also discussed.1

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Section: Introductionmentioning

confidence: 99%

Properties of sodium-driven bacterial flagellar motor: A two-state model approach

Zhang

2015

Mod. Phys. Lett. B

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“…(2) discrete models, in which the molecular motor is assumed to hop periodically among different chemical states, and the chemical transitions are coupled with mechanical motion [40][41][42][43][44][45][46][47][48][49][50]; (3) mechanical models, which try to understand motor mechanism from its mechanical features [51][52][53][54][55]. The continuous models are usually analyzed by biomathematicians and biophysicists to get the qualitative properties of the molecular motor, and the discrete models are usually employed by biologists and biochemists due to their convenience of fitting to experimental data.…”

Section: Introductionmentioning

confidence: 99%

The load dependence of the physical properties of a molecular motor

Meng¹,

Yu²,

Zhang³

2013

J. Phys.: Condens. Matter

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The physical properties of a molecular motor with load changing in a wide range will be discussed in this study, in particular the mean velocity, output power and energy efficiency. The main difficulty of this study is that both the states of the molecular motor and the energy barriers between them change with the loading force. Moreover, with the change of load, the number of motor states may also change, so different models should be used to calculate the corresponding physical quantities in different ranges of load. The results show that, in contrast to the usual intuition, the mean velocity and output power of the molecular motor do not change continuously with load.

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