Li Zilong, Ohki Yasuhiro, Tatsumi Kazuyuki
Research Center for Materials Science and Department of Chemistry, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
J Am Chem Soc. 2005 Jun 29;127(25):8950-1. doi: 10.1021/ja051590+.
[NiFe] hydrogenase, the enzyme of which catalyzes the reversible oxidation of molecular hydrogen to protons and electrons, contains a unique heterodinuclear thiolate-bridged Ni-Fe complex in which the iron center is coordinated by CO and CN. We have synthesized dithiolate-bridged Ni-Fe complexes bearing CO and CN ligands to model the active center of [NiFe] hydrogenase. The Ni-Fe complexes containing a [(CN)2(CO)2Fe(mu-S2)NiS2] framework are the closest yet structural models of [NiFe] hydrogenase.
[镍铁]氢化酶可催化分子氢可逆氧化为质子和电子,其活性中心含有独特的由硫醇盐桥连的异双核镍 - 铁配合物,其中铁中心由一氧化碳和氰根配位。我们合成了带有一氧化碳和氰根配体的二硫醇盐桥连镍 - 铁配合物,以模拟[镍铁]氢化酶的活性中心。含有[(CN)2(CO)2Fe(μ - S2)NiS2]骨架的镍 - 铁配合物是迄今最接近[镍铁]氢化酶的结构模型。