Ogo Seiji, Kabe Ryota, Uehara Keiji, Kure Bunsho, Nishimura Takashi, Menon Saija C, Harada Ryosuke, Fukuzumi Shunichi, Higuchi Yoshiki, Ohhara Takashi, Tamada Taro, Kuroki Ryota
Center for Future Chemistry, Kyushu University, Fukuoka 819-0395, Japan.
Science. 2007 Apr 27;316(5824):585-7. doi: 10.1126/science.1138751.
Models of the active site in [NiFe]hydrogenase enzymes have proven challenging to prepare. We isolated a paramagnetic dinuclear nickel-ruthenium complex with a bridging hydrido ligand from the heterolytic cleavage of H2 by a dinuclear NiRu aqua complex in water under ambient conditions (20 degrees C and 1 atmosphere pressure). The structure of the hexacoordinate Ni(mu-H)Ru complex was unequivocally determined by neutron diffraction analysis, and it comes closest to an effective analog for the core structure of the proposed active form of the enzyme.
已证明制备[NiFe]氢化酶活性位点的模型具有挑战性。我们在环境条件（20摄氏度和1个大气压）下，通过双核NiRu水合络合物在水中对H₂进行异裂，分离出了一种具有桥连氢化物配体的顺磁性双核镍 - 钌络合物。通过中子衍射分析明确确定了六配位Ni(μ-H)Ru络合物的结构，它最接近所提出的酶活性形式核心结构的有效类似物。
