Shedding new light on enzyme crucial to life processes

Researchers at the University of Liverpool have revealed the crystal structure of a bacterial enzyme that offers clues on how electrons in the body move from one protein molecule to another. The movement of electrons is called electron transfer (ET) and is essential for all living organisms, as it underpins processes such as respiration, photosynthesis, and detoxification. Scientists at Liverpool have examined the structure of a natural complex of the electron donor domain and the enzyme, called nitrite reductase, core. The research sheds new light on the role it plays in electron transfer, as well as the production of nitric oxide, a direct precursor to nitrous oxide, which is an ozone-depleting and greenhouse gas, 300 times more potent than carbon dioxide. Dr Svetlana Antonyuk , from the University's Institute of Integrative Biology , explains: "The transfer of electrons between partner proteins is key to the functioning of all living things, but our understanding of how this process occurs is limited. "The protein complexes are very transient in nature so it is not easily possible to obtain their crystals and use the powerful method of crystallography to image them. Our system offered major advantage as it had both the donor and acceptor proteins fused together naturally.