Selenium-bridged diiron hexacarbonyl complexes as biomimetic models for the active site of Fe-Fe hydrogenases.
Three N-substituted selenium-bridged diiron complexes [{(mu-SeCH2)2NC6H4R}Fe2(CO)6] (R = 4-NO2, 7; R = H, 8; R = 4-CH3, 9) were firstly prepared as biomimetic models for the Fe-Fe hydrogenases active site. Models could be generated by the convergent reaction of [(mu-HSe)2Fe2(CO)6] (6) with N,N-bis(hydroxymethyl)-4-nitroaniline (1), N,N-bis(hydroxymethyl)aniline (2), and N,N-bis(hydroxymethyl)-4-methylaniline (3) in 46-52% yields. All the new complexes were characterized by IR, 1H and 13C NMR and HRMS spectra and their molecular structures were determined by single-crystal X-ray analysis. The redox properties of and their dithiolate analogues [{(mu-SCH2)2NC6H4R}Fe2(CO)6] (R = 4-NO2, 7s; R = H, 8s; R = 4-CH3, 9s ) were evaluated by cyclic voltammograms. The electrochemical proton reduction by and were investigated in the presence of p-toluenesulfonic acid (HOTs) to evaluate the influence of changing the coordinating S atoms of the bridging ligands to Se atoms on the electrocatalytic activity for proton reduction.
Gao
Shang
S
State Key Laboratory of Fine Chemicals, Dalian University of Technology, Zhongshan Road 158-40, Dalian, 116012, PR China.
Fan
Jiangli
J
Sun
Shiguo
S
Peng
Xiaojun
X
Zhao
Xing
X
Hou
Jun
J
D001665:Binding Sites; D032701:Biomimetics; D004563:Electrochemistry; D006864:Hydrogenase / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008954:Models, Biological; D008958:Models, Molecular; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D010084:Oxidation-Reduction; D012643:Selenium / Q000737:chemistry*
D007506:Iron-Sulfur Proteins; D009942:Organometallic Compounds; D007501:Iron; C118830:iron hydrogenase; D006864:Hydrogenase; D012643:Selenium