Some reactions of R3SnM（CO）5 （M = Mn, Re） with CH3CN or pyridine were investigated to give complexes R3SnMn（CO）3LL＇ or R3SnMn（CO）4L by a facile mild method. X-ray diffractions analyses show that, in contrast ...Some reactions of R3SnM（CO）5 （M = Mn, Re） with CH3CN or pyridine were investigated to give complexes R3SnMn（CO）3LL＇ or R3SnMn（CO）4L by a facile mild method. X-ray diffractions analyses show that, in contrast to the phosphine ligand occupying in axial position, nitrogen ligands occupy equatorial position.展开更多
Hydrogenases are enzymes that can reversibly split molecular hydrogen. Study on the structure of the active site and the mechanism of catalysis has drawn great attention because the results may be useful for the desig...Hydrogenases are enzymes that can reversibly split molecular hydrogen. Study on the structure of the active site and the mechanism of catalysis has drawn great attention because the results may be useful for the design of cheap biomimetic hydrogen catalysts for fuel cells, or as model for the photoproduction of H\-2. At one time the active site was generally considered to be composed of mononuclear nickel complex with ligands from the polypeptide. A breakthrough in the understanding of the structure of Hases occurred with the resolution crystal structure of D. gigas Hases in 1995. The unexpected result challenged the previously reported spectroscopic studies and caused some academic arguments. Some methods and results used for insight into Hases have to be reconsidered. Different viewpoints concerning the structure of active site of Hases in different periods and some remaining questions will be presented.展开更多
基金supported by the National Natural Science Foundation of China(No.29672018).
文摘Some reactions of R3SnM（CO）5 （M = Mn, Re） with CH3CN or pyridine were investigated to give complexes R3SnMn（CO）3LL＇ or R3SnMn（CO）4L by a facile mild method. X-ray diffractions analyses show that, in contrast to the phosphine ligand occupying in axial position, nitrogen ligands occupy equatorial position.
文摘Hydrogenases are enzymes that can reversibly split molecular hydrogen. Study on the structure of the active site and the mechanism of catalysis has drawn great attention because the results may be useful for the design of cheap biomimetic hydrogen catalysts for fuel cells, or as model for the photoproduction of H\-2. At one time the active site was generally considered to be composed of mononuclear nickel complex with ligands from the polypeptide. A breakthrough in the understanding of the structure of Hases occurred with the resolution crystal structure of D. gigas Hases in 1995. The unexpected result challenged the previously reported spectroscopic studies and caused some academic arguments. Some methods and results used for insight into Hases have to be reconsidered. Different viewpoints concerning the structure of active site of Hases in different periods and some remaining questions will be presented.
