中性子結晶解析の進展が明らかにする酵素反応機構

抄録

Neutron crystallography enables direct observation of hydrogen atoms which play crucial roles in the physiological functions of enzymes, including molecular recognition through hydrogen bonding and catalytic reactions involving proton-coupled electron transfer. Now neutron crystallography is a limited method for protein structure determination, but steadily catholicizes with an operation of diffractometers for bio-macromolecules at neutron facilities and accumulated techniques for sample preparation. In this article, we give a commentary on the current status of neutron crystallography for bio-macromolecules in the world, and illustrate our recent results, neutron structural analyses of copper amine oxidase and copper-containing nitrite reductase, which provide in-depth understandings of the enzymatic reaction mechanism.