@article{oai:repo.qst.go.jp:00083163,
 author = {河野, 史明 and 栗原, 和男 and 玉田, 太郎 and Fumiaki, Kono and Kazuo, Kurihara and Taro, Tamada},
 issue = {4},
 journal = {生物物理},
 month = {Jul},
 note = {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.},
 pages = {216--222},
 title = {中性子結晶解析の進展が明らかにする酵素反応機構},
 volume = {61},
 year = {2021}
}