The data to the right were collected for the myosin-catalyzed hydrolysis of ATP. Use these data to determine the values of Rmax (the maximum rate of the enzyme, often called the maximum velocity, Vmax) and KM, the Michaelis-Menten constant. Answer the four parts below.

Calculate the maximum work available from 35.0 g of aluminum in the following cell when the cell potential is 1.23 V: Al(s) | Al³+ (aq) || H+ (aq) | O2(g) | Pt Note that O2 is reduced to H2O. Maximum work =

Which of the following statements are true about the relationships of [S], KM, and Vmax?  (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.

Some enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics? (Please show work and correct answer)

In active muscle cells, the pO2 is about 10 torr at the cell surface and 1 torr at the mitochondria(the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygentransported to the mitochondria of muscle cells by myoglobin (KD = 2 torr).

From a series of flasks with a constant concentration of enzyme the following initial velocities weretaken, they were obtained as a function of the concentration of the substrate.a) Calculate the KM and Vmax kinetic parameters of the three forms (Lineweaver-Burk, Eadie-Hofstee, Dixon).b) Analyze which are the atypical data that cause a low correlation, which can be eliminated and explain youranswer.

When the Cu2+ concentration is 1.01 M, the observed cell potential at 298K for an electrochemical cell with the following reaction is 1.138V. What is the Cr3+ concentration? 3Cu2(aq) + 2Cr(s) 3Cu(s) + 2Cr3+(aq) Answer: M

If you want to determine the KM for lactate, what protocol do you set up? Discuss the significance of the following kinetic parameters that are used to characterize enzyme activity: KM, Vmax, kcat, and kcat / KM.

Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Na*-glucose symporter. Recall that the Na+ concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Na+ ions into the cell to the "uphill" transport of glucose into the cell. If the Na+ concentration outside the cell ([Na* lout) is 147 mM and that inside the cell ([Na+]in) is 17.0 mM, and the cell potential is -54.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. AG gluc kJ mol What is the maximum ratio of [glucose]in to [glucose] out that could theoretically be produced if the energy coupling were 100% efficient? 1.13 2.3 × 10-4 8.36 4300