Final answer:
The maximal turnover rate of ATP hydrolysis by a kinesin molecule's motor domain cannot be determined from the provided information without knowing the specific energy use per 'step' of the kinesin on a microtubule. Kinesin is an ATPase, and movement rates and ATP consumption typically require empirical measurement.
Step-by-step explanation:
To determine the maximal turnover rate of ATP molecules hydrolyzed per second by one motor domain of a kinesin molecule, we must consider the energy requirements of kinesin's movement along microtubules and the energy provided by the hydrolysis of ATP. Motor proteins like kinesin are ATPases, using the free energy from ATP hydrolysis to fuel their movement and transport cellular cargo.
Given that the hydrolysis of one ATP molecule releases 7.3 kcal/mol of energy and a motor protein like kinesin utilizes this energy, we must understand how much energy it takes for kinesin to 'walk' and carry out its function. For example, it requires 2.1 kcal/mol of energy to move one Na+ across a membrane, giving us a framework for understanding ATP usage; however, the specific ATP consumption rate for kinesin movement has not been directly provided in the question.
Without additional specific information about energy per step for kinesin, we cannot calculate an exact turnover rate. Typically, scientific studies measure kinesin's ATPase activity to establish such a rate. It's also notable that the turnover rate can vary depending on specific conditions, such as the presence of cargo and the type of microtubule track.