What type of bonding typically occurs between proteins and coenzymes?

Proteins and coenzymes commonly interact through hydrogen bonding, among other interactions. Hydrogen bonds are crucial because they are relatively weak and can allow for dynamic and reversible interactions between the protein and the coenzyme. This reversibility is essential in biological systems, where the binding of a coenzyme to an enzyme must be regulated and adaptable to various cellular conditions and metabolic needs.

In the context of enzyme activity, coenzymes often assist in facilitating biochemical reactions by transiently binding to the active site of an enzyme. The formation of hydrogen bonds helps stabilize the binding between the coenzyme and the enzyme, enabling the necessary structural changes to progress through the reaction pathway.

While covalent bonding might occur in specific scenarios involving more permanent modifications or links, most interactions between proteins and coenzymes are characterized by non-covalent interactions to maintain flexibility. Ionic bonding and Van der Waals forces can also play a role; however, hydrogen bonding is more prevalent and critical for the transient interactions that define the function of many enzymes and their coenzymes.