Hi Sara,
From what I know, reversible inhibition occurs when the inhibitor binds to the enzyme’s active site via a non-covalent interaction (i.e. H-bonds, hydrophobic bonds, and other intramolecular interactions). With non-covalent bonds, it is temporary, so the inhibitor could basically get knocked-off by a substrate or another inhibitor that more specifically binds to the active site (as seen in competitive inhibition, which is relieved by increasing # of substrates). As for irreversible inhibition, the inhibitor forms covalent bonds with the enzyme’s active site. Covalent bonds are intramolecular interactions (e.g. the bond between two chloride atoms to make Cl2, and the double bond between two oxygen atoms to make O2). These are stronger that non-covalent bonds, which explains why it is irreversible. As for examples, toxins are usually common irreversible inhibitors.
Hope these help!