(This article is based on information from Technology Foundation STW)
Researchers from the United States, Thailand, the Netherlands (including the Laboratory of Biochemistry at Wageningen University) and Italy have discovered how oxygen reaches the active centre of enzymes in a widely used enzyme model. It turned out that oxygen travels through various tunnels through the protein layer of the enzyme, but these tunnels ultimately all end up at the same entryway to the active centre. These insights will help to improve existing oxidative enzymes or create new ones. Such enzymes can be adapted to catalyse new, environmentally benign chemical processes. The researchers published their findings in the journal Proceedings of the National Academy of Sciences (PNAS).
Enzymes are extremely effective catalysts that can be used in a wide range of applications. However, for each application an enzyme with specific properties is required. The availability of natural enzymes that are suitable for these processes is limited. Consequently, there is great interest in genetically modified enzymes. Although a powerful methods have been developed for creating such enzymes, it is still an extremely complex process to create enzymes with the specific properties that are desired.
Applied work has shown that mutations in the active centre of an enzyme are especially effective. This requires thorough knowledge of the functioning of the active centre. Many enzymes require oxygen to function. The active centre of such enzymes is usually hidden inside the enzyme. Until recently, it was unclear how these enzymes '"breathe": how can oxygen molecules reach the active centres without a molecular navigation system? Does this take place by random diffusion through the protein layer of the enzyme, or along one or more specific tunnels for oxygen transport? The answer to this question was unclear.