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Here we generalize our previous model of molecular motors traffickingsubdiffusing cargos in viscoelastic cytosol by (i) including mechanochemicalcoupling between cyclic conformational fluctuations of the motor protein drivenby the reaction of ATP hydrolysis and its translational motion within thesimplest two-state model of hand-over-hand motion of kinesin, and also (ii) bytaking into account the anharmonicity of the tether between the motor and cargo(its maximally possible extension length). It is shown that the major earlierresults such as occurrence of normal versus anomalous transport depending onthe amplitude of binding potential, cargo size and the motor turnover frequencynot only survive in this more realistic model, but the results also look verysimilar for the correspondingly adjusted parameters. However, this morerealistic model displays a substantially larger thermodynamic efficiency due toa bidirectional mechanochemical coupling. For realistic parameters, the maximalthermodynamic efficiency can be transiently about 50% as observed for kinesins,and even larger, surprisingly also in a novel strongly anomalous (sub)transportregime, where the motor enzymatic turnovers become also anomalously slow andcannot be characterized by a turnover rate. Here anomalously slow dynamics ofthe cargo enforces anomalously slow cyclic kinetics of the motor protein.

Anomalous transport of subdiffusing cargos by single kinesin motors: the role of mechanochemical coupling and anharmonicity of tether