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Report No.
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Preliminary neutron diffraction experiments of electron transfer proteins

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

Most of electron transfer proteins possess prosthetic groups, such as heme, flavin and iron-sulfur cluster, and electron transfer reaction is mediated by hydrogen atoms or valence shell electrons of the prosthetic groups. Therefore, structural information including hydrogen atoms is required for understanding their electron transfer mechanisms. We have performed high-resolution neutron structure analyses with 2 electron transfer proteins of high-potential iron-sulfur protein (HiPIP) and NADH-cytochrome ${it b5}$ reductase (b5R). Diffraction experiments were performed at BL03 (iBIX) beamline of J-PARC using large crystals of HiPIP and b5R. Diffraction spots were observed up to 1.17 ${AA}$ and 1.37 ${AA}$ resolutions for HiPIP and b5R, respectively.

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