The question asks what happens in the Michaelis-Menten equation when the drug concentration C equals the Michaelis constant Km. Let's check each option against the mathematics of the equation.
Direct substitution of C equal to Km into the Michaelis-Menten equation shows the rate becomes exactly half the maximum rate, which is in fact the condition used to determine Km experimentally.
Therefore, the correct answer is the rate of process is equal to half of maximum rate.

| List I Name of Vitamin | List II Functions of Vitamins | ||
| A | Riboflavin | I | The electron acceptor for isocitrate dehydro- genase |
| B | Niacin | II | Decarboxylation of alpha-ketoglutarate dehydrogenas |
| C | Thiamine | III | Part of coenzyme A |
| D | Pantothenic acid | IV | Cofactor for succinate dehydrogenase |
| V | Enzyme activity regulator, such as for protein kinase C |
List I | List II | ||
|---|---|---|---|
| A | \(\Omega^{-1}\) | I | Specific conductance |
| B | \(∧\) | II | Electrical conductance |
| C | k | III | Specific resistance |
| D | \(\rho\) | IV | Equivalent conductance |
List I | List II | ||
|---|---|---|---|
| A | Constant heat (q = 0) | I | Isothermal |
| B | Reversible process at constant temperature (dT = 0) | II | Isometric |
| C | Constant volume (dV = 0) | III | Adiabatic |
| D | Constant pressure (dP = 0) | IV | Isobar |