Spectroscopic and crystallographic evidence for the N-protonated FeIFeI azadithiolate complex related to the active site of Fe-only hydrogenases.
The complex [{(mu-SCH2)2N(CH2C6H4-2-Br)}Fe2(CO)6] and its N-protonated species, as structural models of the Fe-only hydrogenase active site, were identified spectroscopically and crystallographically, and their molecular structures show the 0.04-0.1 A lengthening of the three N-C bonds and an intramolecular HBr contact (2.82 Angstroms) in the crystalline state of the N-protonated species.
Wang
Fujun
F
State Key Laboratory of Fine Chemicals, Dalian University of Technology, Dalian, P. R. China.
Wang
Mei
M
Liu
Xiaoyang
X
Jin
Kun
K
Dong
Weibing
W
Li
Guanghua
G
Akermark
Björn
B
Sun
Licheng
L
D001665:Binding Sites; D003461:Crystallography; D006864:Hydrogenase / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011522:Protons; D013055:Spectrophotometry, Infrared; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D007506:Iron-Sulfur Proteins; D011522:Protons; D013438:Sulfhydryl Compounds; C118830:iron hydrogenase; D006864:Hydrogenase