@misc{oai:repo.qst.go.jp:00078365,
 author = {Hiromoto, Takeshi and Nishikawa, Koji and Matsuura, Hiroaki and Hirano, Yu and Kusaka, Katsuhiro and Cuneo, Matthew and Tamada, Taro and Higuchi, Yoshiki and Hiromoto, Takeshi and Hirano, Yuu and Tamada, Taro},
 month = {Oct},
 note = {Hydrogenases that catalyze the reversible oxidation of molecular hydrogen (H2) are involved in energy metabolism in various prokaryotes and some eukaryotes. The “standard” type of [NiFe]-hydrogenases is composed of two (large and small) subunits. The active site Ni-Fe binuclear complex of the “standard” enzyme is located in the protein interior at the interface of the two subunits by coordination of four cysteine residues of the large subunit. In order to clarify how the inactive oxidized form is re-activated by H2 and to observe a bridged hydride in the Ni-Fe complex in the Ni-R form directly, structural analyses using neutron diffraction were undertaken on the crystals prepared in aerobic and anaerobic conditions, respectively., International Symposium on Diffraction Structure Biology 2019},
 title = {Neutron diffraction experiments on [NiFe]-hydrogenase crystallized under H2 atmosphere},
 year = {2019}
}