What distinguishes reversible inhibitors from irreversible inhibitors?

Reversible inhibitors are characterized by their ability to bind to enzymes through non-covalent interactions, such as hydrogen bonds, ionic bonds, and hydrophobic interactions. These interactions are typically weak and transient, meaning that the inhibitor can dissociate from the enzyme and allow it to return to its normal function. This binding feedback loop allows for the regulation of enzymatic activity depending on the concentration of the inhibitor present.

In contrast, irreversible inhibitors form covalent bonds or strong interactions with the enzyme, leading to permanent inactivation. Because of this permanent modification, the enzyme cannot be restored to its active form simply by removing the inhibitor. Consequently, the correct answer highlights the temporary nature of reversible inhibitors, making them fundamentally different from irreversible inhibitors that permanently deactivate enzymes.