Dithiolato-bridged dinuclear iron-nickel complexes [Fe(CO)2(CN)2(mu-SCH2CH2CH2S)Ni(S2CNR2)]- modeling the active site of [NiFe] hydrogenase.
[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.
Li
Zilong
Z
Research Center for Materials Science and Department of Chemistry, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
Ohki
Yasuhiro
Y
Tatsumi
Kazuyuki
K
D001665:Binding Sites; D018360:Crystallography, X-Ray; D006864:Hydrogenase / Q000138:chemical synthesis / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D009532:Nickel / Q000737:chemistry*; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*
D009942:Organometallic Compounds; D009532:Nickel; D007501:Iron; D006864:Hydrogenase