Synthesis and structure of analogues for the Ni-Fe site in hydrogenase enzymes.
Dithiolate bridging Ni-Fe complexes [(dppe)Ni(II)(mu-SEt)(2)Fe(II)(CN)(2)(CO)(2)](6) and [(dppe)Ni(II)(mu-pdt)Fe(II)(CN)(2)(CO)(2)] [dppe = 1,2-bis(diphenylphosphino)ethane and pdt = 1,3-propanedithiolate] have been synthesized and structurally characterized as structural analogues of the active site of Ni-Fe hydrogenase enzymes. The synthesis starts from key intermediate fac-[Fe(CN)(2)(CO)(3)I](-). [(dppe)Ni(II)(mu-SEt)(2)Fe(II)(CN)(2)(CO)(2)](6), which features a near-planar diethanethiolate-bridged Ni-Fe rhomb, and the arrangement of 2CN(-) ligands is cis to each other. In contrast, [(dppe)Ni(II)(mu-pdt)Fe(II)(CN)(2)(CO)(2)] shows a much more folded NiS(2)Fe rhomb, a short Ni-Fe distance, trans 2CN(-) ligands, and a semibridging CN(-) between Ni and Fe.
Jiang
Jianfeng
J
Department of Chemistry, Yeshiva University, New York, New York 10033, USA. Jiang@yu.edu
Maruani
Myriam
M
Solaimanzadeh
Jonathan
J
Lo
Wenfeng
W
Koch
Stephen A
SA
Millar
Michelle
M
D020134:Catalytic Domain; D006864:Hydrogenase / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular
C043296:nickel-iron hydrogenase; D006864:Hydrogenase