The g factors g||,g⊥ and hyperfine structure constants A||,A⊥ for two trigonal Co^2+ centers (i.e.,Co^2+ in Cd^2+ (I) and Cd^2+ (Ⅱ) sites) in CsCdCl3:Co^2+ crystals are calculated from the high-order perturbation f...The g factors g||,g⊥ and hyperfine structure constants A||,A⊥ for two trigonal Co^2+ centers (i.e.,Co^2+ in Cd^2+ (I) and Cd^2+ (Ⅱ) sites) in CsCdCl3:Co^2+ crystals are calculated from the high-order perturbation formulas based on the cluster approach.In the calculation,the contributions from covalency effect and configuration interaction effect are considered and the parameters related to both effects are obtained from the optical spectrum and the structure data of the studied system.The results are in good agreement with the observed values.展开更多
The glucose isomerase(GI) was a metal activating enzyme It was most activated by Co 2+ and Mg 2+ ,and Mg 2+ was the best activator,whether the glucose or the xylose was the substrate When the glucose was substrate,the...The glucose isomerase(GI) was a metal activating enzyme It was most activated by Co 2+ and Mg 2+ ,and Mg 2+ was the best activator,whether the glucose or the xylose was the substrate When the glucose was substrate,the dissociation constant of Mg 2+ GI,Co 2+ GI and Mn 2+ -GI was 115 μmol/L,40 μmol/L, and 15 μmol/L respectively. The maximum activity of Mg 2+ GI,Co 2- GI and Mn 2+ GI was 100%,85%,and 20% respectively. When the xylose was substrate,the order of dissociation constant and maximum activity of the metal enzymes was the same Ca 2+ was a competitive inhibitor versus Mg 2+ ( K i 7 4 μmol/L)or Co 2+ ( K i 99 μmol/L). Compared with Mg 2+ GI,the K m of Co 2+ GI was more,and the V M of Co 2+ GI less The process of activity recovery from apo GI to metal GI showed that it was slow and of two展开更多
文摘The g factors g||,g⊥ and hyperfine structure constants A||,A⊥ for two trigonal Co^2+ centers (i.e.,Co^2+ in Cd^2+ (I) and Cd^2+ (Ⅱ) sites) in CsCdCl3:Co^2+ crystals are calculated from the high-order perturbation formulas based on the cluster approach.In the calculation,the contributions from covalency effect and configuration interaction effect are considered and the parameters related to both effects are obtained from the optical spectrum and the structure data of the studied system.The results are in good agreement with the observed values.
文摘The glucose isomerase(GI) was a metal activating enzyme It was most activated by Co 2+ and Mg 2+ ,and Mg 2+ was the best activator,whether the glucose or the xylose was the substrate When the glucose was substrate,the dissociation constant of Mg 2+ GI,Co 2+ GI and Mn 2+ -GI was 115 μmol/L,40 μmol/L, and 15 μmol/L respectively. The maximum activity of Mg 2+ GI,Co 2- GI and Mn 2+ GI was 100%,85%,and 20% respectively. When the xylose was substrate,the order of dissociation constant and maximum activity of the metal enzymes was the same Ca 2+ was a competitive inhibitor versus Mg 2+ ( K i 7 4 μmol/L)or Co 2+ ( K i 99 μmol/L). Compared with Mg 2+ GI,the K m of Co 2+ GI was more,and the V M of Co 2+ GI less The process of activity recovery from apo GI to metal GI showed that it was slow and of two
