@misc{oai:repo.qst.go.jp:00079970,
 author = {Hirano, Yuu and Kurihara, Kazuo and Kusaka, Katsuhiro and Ostermann, Andreas and Kimura, Shigenobu and Miki, Kunio and Tamada, Taro and Hirano, Yuu and Kurihara, Kazuo and Tamada, Taro},
 month = {Dec},
 note = {Information about hydrogen atoms and valence electrons is important to understand functions of electron transfer proteins, because they are directly connected with the reactivity of redox reactions. In the redox proteins, the possibility of quantum tunneling has been discussed on the hydrogen and electron transfer reactions. Therefore, high-resolution structural information is required to detect small structural changes due to the redox reactions. The NADH-cytochrome b5 reductase (b5R) and cytochrome b5 (b5) redox system is involved in various electron transfer reactions, such as lipid unsaturation, cholesterol synthesis and drug metabolism. The X-ray crystal structure of oxidized form of b5R at 0.78 Å resolution clearly visualized valence electron densities of the FAD cofactor. The X-ray crystal structures of the oxidized and reduced forms of b5 shows small structural changes between two redox states. We have recently determined the neutron crystal structures of the oxidized form of b5R at 1.4 Å resolution. In addition, we have determined high-resolution X-ray crystal structures of the reduced form of b5R. The neutron and X-ray structure analyses provide information about the hydrogen transfer pathway in b5R., 3rd QST International Symposium},
 title = {Structural studies of the NADH-cytochrome b5 reductase},
 year = {2019}
}