Tunneling of intermediates in enzyme-catalyzed reactions

A fascinating group of enzymes has been shown to possess multiple active sites connected by intramolecular tunnels for the passage of reactive intermediates from the site of production to the site of utilization. In most of the examples studied to date, the binding of substrates at one active site enhances the formation of a reaction intermediate at an adjacent active site. The most common intermediate is ammonia, derived from the hydrolysis of glutamine, but molecular tunnels for the passage of indole, carbon monoxide, acetaldehyde and carbamate have also been identified. The architectural features of these molecular tunnels are quite different from one another, suggesting that they evolved independently.