Using POE, I know that the major difference between reversible and irreversible inhibition is that irreversible involves strong covalent bonds. This means A and D are out. From the graph, you can see that more inhibitor is required for the same activity if it is not pre-incubated, so B is out.
You should know, however, that for irreversible inhibition, the kinetics are not dependent on Km values but rather on how long the enzyme in question has been pre-incubated with the irreversible inhibitor. So there's something called kobs which is essentially the plot of enzyme activity vs. time, which when plotted logarithmically resembles first-order decay. So you use kobs/ as the x-axis rather than Km.
Basically, just know that for irreversible inhibition, that kinetics are time-dependent, so you cannot use MM kinetics to describe them. Also, you cannot recover enzyme activity by diluting out the inhibitor. You can only synthesize more enzyme.