Final answer:
The free dissociation of an inhibitor from an enzyme without covalent bonding is characteristic of reversible inhibition. In this context, competitive and noncompetitive inhibitors both demonstrate reversible association with enzymes, but competitive inhibition is specifically dependent on the inhibitor's competition with the substrate for the enzyme's active site.
Step-by-step explanation:
The free dissociation of an inhibitor from an enzyme, meaning that the inhibitor can leave the enzyme without a permanent bond being formed, is typical of reversible inhibition. The correct answer is (d) reversible inhibition. Competitive inhibition is a form of reversible inhibition where the inhibitor competes for the enzyme's active site, which is also where the substrate would bind. Thus, competition ensues between the substrate and inhibitor for the active site, but since this is a reversible process, the inhibitor can dissociate freely, making room for the substrate to eventually bind. Noncompetitive inhibition also involves reversible binding, but in this case, the inhibitor does not compete for the active site because it binds to a different part of the enzyme. This is why the addition of more substrate does not reverse the inhibitory effect in noncompetitive inhibition.