A proton-hydride diiron complex with a base-containing diphosphine ligand relevant to the [FeFe]-hydrogenase active site.
A diiron dithiolate complex holding a mu-hydride on the iron atoms and a proton on the basic site of a chelating diphosphine ligand was prepared and crystallographically characterized as a structural model of the [FeFe]-hydrogenase active site, and its molecular structure shows the H(mu)(-)...H(N)(+) distance is 3.934 A.
Wang
Ning
N
State Key Laboratory of Fine Chemicals, DUT-KTH Joint Education and Research Centre on Molecular Devices, Dalian University of Technology, Dalian, 116012, China.
Wang
Mei
M
Zhang
Tingting
T
Li
Ping
P
Liu
Jihong
J
Sun
Licheng
L
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005290:Ferric Compounds / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D010720:Phosphines / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D005290:Ferric Compounds; D007506:Iron-Sulfur Proteins; D008024:Ligands; D010720:Phosphines; D013438:Sulfhydryl Compounds; C002007:dithiol-iron(III)-sulfide complex; C118830:iron hydrogenase; D006864:Hydrogenase; C044646:phosphine