What type of bond is formed between an enzyme and a strong inhibitor?

The bond formed between an enzyme and a strong inhibitor is a covalent bond. This type of bond is characterized by the sharing of electron pairs between atoms, which creates a stable connection. In the context of enzyme inhibition, strong inhibitors typically interact with the active site of the enzyme by forming a covalent bond, thereby permanently altering the enzyme's structure or functionality. This permanent modification prevents the enzyme from performing its catalytic function, leading to effective inhibition.

Covalent bonds are often associated with irreversible inhibitors, which permanently bind to the enzyme through a covalent interaction. This contrasts with weaker interactions, such as hydrogen bonds, ionic bonds, or disulfide bonds, which may result in temporary binding and can often be reversed, allowing the enzyme to regain its activity once the inhibitor is removed. Thus, the formation of a covalent bond indicates a strong and lasting interaction between the enzyme and the inhibitor.