Metal ion catalysis

Metal ion catalysis is a chemical mechanism in which enzymes utilize various metal ions—either tightly bound as prosthetic groups or loosely associated as cofactors—to facilitate the catalysis of biochemical reactions[1][2][3][4][10]. These metal ions may activate substrates through Lewis acid chemistry, stabilize negative charges or transition states, or function in redox reactions and electron transfer. Common examples are found in enzymes such as carbonic anhydrase (zinc-dependent)[6], cytochrome c oxidase (iron/copper-dependent)[2], and carboxypeptidase A (zinc-dependent)[1][4]. Metal ion catalysis is essential for the function of about one-third of all known enzymes[10], but as a concept, it is not a unique protein or molecular target for drugs. Rather, many different metalloenzymes utilize this principle in their distinct biological roles. Thus, while "Metal ion catalysis" can be discussed in terms of its mechanism, specific therapeutic targeting requires focus on individual metalloenzymes employing this strategy.

Other names

Metal ion catalysisMetalloenzyme catalysisMetal-mediated catalysis