Which of the following is an example of reversible inhibition?

Reversible inhibition is characterized by the ability of an inhibitor to bind to an enzyme temporarily, typically through non-covalent interactions such as hydrogen bonds, ionic bonds, or hydrophobic interactions. This temporary binding allows the enzyme to regain its activity once the inhibitor is removed, distinguishing it from irreversible inhibition, where inhibition continues even after the inhibitor is removed due to covalent bonds or other permanent changes.

The choice highlighting short-term binding accurately reflects the essence of reversible inhibition. In reversible inhibition, the inhibitor forms temporary associations with the enzyme, leading to a temporary decrease in enzyme activity that can be undone. This is a key feature of reversible inhibitors, as they do not permanently alter the enzyme's structure or function.

Conversely, iodine binding typically involves more stable associations that may not fit the criteria of reversible inhibition, while covalent bond formation represents a form of irreversible inhibition, leading to permanent changes in the enzyme's structure. Enzyme mutation can also alter enzyme activity permanently and is not related to reversible inhibition processes.