A Convenient Route to Synthetic Analogues of the Oxidized Form of High-Potential Iron-Sulfur Proteins

作者：Tanifuji Kazuki; Yamada Norihiro; Tajima Tomoyuki; Sasamori Takahiro; Tokitoh Norihiro; Matsuo Tsukasa; Tamao Kohei; Ohki Yasuhiro; Tatsumi Kazuyuki^*

来源：Inorganic Chemistry, 2014, 53(8): 4000-4009.

DOI：10.1021/ic402890k

An amide-bound [Fe4S4](3+). cluster, [Fe4S4{N-(SiMe3)(2)}(4)](-) (1), was found to serve as a convenient precursor for synthetic analogues of the oxidized form of high-potential iron sulfur proteins. Treatment of 1 with 4 equiv of bulky thiols led to replacement of the amide ligands with thiolates, giving rise to a series of [Fe4S4(SR)(4)](-) clusters (R = Dmp (2a), Tbt (2b), Eind (2c), Dxp (2d), Dpp (2e); Dmp = 2,6-di(mesityl)phenyl, Tbt = 2,4,6-tris[bis(trimethylsily)methyl]phenyl, Eind = 1,1,3,3,5,5,7,7-octaethyl-s-hydrindacen-4-yl, Dxp = 2,6-di(m-xylyl)phenyl, Dpp = 2,6-diphenylphenyl). These clusters were characterized by the mass spectrum, the EPR spectrum, and X-ray crystallography. The redox potentials of the [Fe4S4](3+/2+) couple, -0.82 V (2a), -0.86 V (2b), -0.84 V (2c), -0.74 V (2d), and -0.63 V (2e) vs Ag/Ag+ in THF, are significantly more negative than that of [Fe4S4(SPh)(4)](-/2-) (-0.21 V).

• 出版日期2014-4-21