Density functional study on dihydrogen activation at the H cluster in Fe-only hydrogenases.
Models simulating the catalytic diiron subcluster [FeFe](H) in Fe-only hydrogenases have often been designed for computational exploration of the catalytic mechanism of the formation and cleavage of dihydrogen. In this work, we extended the above models by explicitly considering the electron reservoir [4Fe-4S](H) which is linked to the diiron subcluster to form a whole H cluster ([6Fe-6S] = [4Fe-4S](H) + [FeFe](H)). Large-scale density functional theory (DFT) computations on the complete H cluster, together with simplified models in which the [4Fe-4S](H) subcluster is not directly involved in the reaction processes, have been performed to probe hydrogen activation on the Fe-only hydrogenases. A new intermediate state containing an Fe(p)...H...CN two-electron three-center bond is identified as a key player in the H2 formation/cleavage processes.
Zhou
Taijin
T
Department of Chemistry, State Key Laboratory for Physical Chemistry of Solid States, Xiamen University, Xiamen, Fujian 361005, PR China. tjzhou@xmu.edu.cn
Mo
Yirong
Y
Zhou
Zhaohui
Z
Tsai
Khirui
K
D001665:Binding Sites; D002384:Catalysis; D016000:Cluster Analysis; D019295:Computational Biology; D003486:Cyanides / Q000737:chemistry; D019281:Dimerization; D004579:Electron Transport; D006859:Hydrogen / Q000737:chemistry* / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D007501:Iron / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
D003486:Cyanides; D007506:Iron-Sulfur Proteins; D006859:Hydrogen; D007501:Iron; C118830:iron hydrogenase; D006864:Hydrogenase