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Oral presentation

Oral presentation

Neutron structural analysis of NADH-cytochrome ${it b$_{5}$}$ reductase

Hirano, Yu; Yamada, Mitsugu*; Kurihara, Kazuo; Shoyama, Yoshinari*; Kuroki, Ryota; Kusaka, Katsuhiro*; Kimura, Shigenobu*; Takeda, Kazuki*; Miki, Kunio*; Tamada, Taro

no journal, , 

NADH-cytochrome ${it b$_{5}$}$ reductase (b5R), a flavoprotein consisting of NADH- and FAD- domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome ${it b$_{5}$}$. The reaction catalyzed by ${it b$_{5}$}$ plays a role in fatty acid synthesis, cholesterol synthesis, and xenobiotic oxidation as a member of the electron transport chain on the endoplasmic reticulum. We have already determined the crystal structures of both the fully reduced and oxidized forms of porcine liver b5R by X-ray crystallography, but, its detail mechanism, especially hydride/proton transfers and exact states of semiquinone, still remains unknown. The hydrogen information obtained by neutron crystallography will be essential for the real understanding of catalytic cycle of the ${it b$_{5}$}$. A large crystal with the size of almost 2 mm$$^{3}$$ was transferred to cryo-protectant solution by stepwise soaking method, and then were flash-frozen in a cold nitrogen gas stream. Using this crystal, we collected neutron data to 1.4${AA}$ resolution at BL03 (iBIX), MLF, J-PARC, and then collected to 0.85${AA}$ resolution at BL5A, PF, KEK. Crystallographic refinement using both neutron and X-ray data is in progress.

Oral presentation

Neutron structure analysis of high-potential iron-sulfur protein

Hirano, Yu; Tamada, Taro; Kurihara, Kazuo; Kusaka, Katsuhiro*; Miki, Kunio*

no journal, , 

High-potential iron-sulfur protein (HiPIP) possesses a 4Fe-4S cluster as a cofactor that shows 2+/3+ redox states. HiPIP is a soluble electron carrier protein that works in the photosynthetic electron transfer chain of purple photosynthetic bacteria. We have determined the neutron crystal structure of HiPIP at high resolution to obtain structure information including hydrogen atoms. Neutron diffraction experiment was performed at J-PARC, and the diffraction data set was obtained at 1.1 ${AA}$ resolution that is the highest resolution in the protein neutron diffraction data. To perform X-ray and neutron joint refinement, we also collected X-ray diffraction data at Photon Factory, and the diffraction data set was obtained at 0.66 ${AA}$ resolution.

Oral presentation

Single crystal neutron diffraction study of high neutron absorbing compound EuX$$_{4}$$ (X = Al, Ga)

Kawasaki, Takuro; Kaneko, Koji; Aso, Naofumi*; Nakamura, Ai*; Hedo, Masato*; Nakama, Takao*; Onuki, Yoshichika*; Moyoshi, Taketo*; Nakao, Akiko*; Hanashima, Takayasu*; et al.

no journal, , 

no abstracts in English

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