@article{oai:repo.qst.go.jp:00047569,
 author = {玉田, 太郎 and 海野, 昌喜（茨城大学大学院理工学研究科） and 日下, 勝弘（茨城大学フロンティア応用原子科学研究センター） and 杉島, 正一（久留米大学医学部） and 和田, 啓（宮崎大学テニュアトラック推進機構） and 萩原, 義徳（久留米工業高等専門学校生物応用化学科） and 福山, 恵一（大阪大学大学院工学研究科） and 玉田 太郎},
 issue = {3},
 journal = {波紋},
 month = {Aug},
 note = {Phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the conversion of　biliverdin (BV) to phycocyanobilin, a light harvesting pigment. To visualize the hydrogens (and protons) in　this unique enzyme, we conducted neutron crystallography of the PcyA-BV complex. In　the enzyme, BV bound to PcyA was in equilibrium between the neutral (BV) and the　protonated (BVH+) forms. Both of the structures including the hydrogen atoms could be　determined. The protonation of the nearby essential residue Asp105 was complemented　with the BV protonation states. His88, an essential residue, was protonated to form a　hydrogen bond to a lactam oxygen of the BV A-ring. His88 is also hydrogen-bonded to　His74 via a hydronium ion. In this article, we also describe the story to grow the large　crystals of the PcyA-BV complex and its neutron diffraction experiment.},
 pages = {130--134},
 title = {ビリン還元酵素PcyAと基質ビリベルジン複合体の中性子結晶構造解析で見えてきたもの},
 volume = {26},
 year = {2016}
}