The crustal and upper mantle azimuthal anisotropy of the Tibetan Plateau and adjacent areas was studied by Rayleigh wave tomography. We collected sufficient broadband digital seismograms trav-ersing the Tibetan Platea...The crustal and upper mantle azimuthal anisotropy of the Tibetan Plateau and adjacent areas was studied by Rayleigh wave tomography. We collected sufficient broadband digital seismograms trav-ersing the Tibetan Plateau and adjacent areas from available stations, including especially some data from the temporary stations newly deployed in Yunnan, eastern Tibet, and western Sichuan. They made an adequate path coverage in most regions to achieve a reasonable resolution for the inversion. The model resolution tests show that the anisotropic features of scope greater than 400 km and strength greater than 2% are reliable. The azimuthal anisotropy pattern inside the Tibetan Plateau was similar to the characteristic of tectonic partition. The crustal anisotropy strength is greater than 2% in most re-gions of East Tibet, and the anisotropy shows clockwise rotation surrounding the eastern Himalayan syntaxis. Vertically, the anisotropy direction indicates a coherent pattern within the upper crust, lower crust, and lithosphere mantle of the Tibetan Plateau, which also is consistent with GPS velocity field and SKS fast polarization directions. The result supports that the crust-mantle deformation beneath the Tibetan Plateau is vertically coherent. The anisotropy strength of crust and lithospheric upper mantle in Yunnan outside the Tibetan Plateau is lower than 2%, so SKS splitting from core-mantle boundary to station should largely be attributed to the anisotropy of asthenosphere.展开更多
The key subunit II of cytochrome c oxidase (CcO) contains a soluble binuclear copper center (CuA) domain. The CUA domain of Paracoccus versutus was cloned, expressed, purified and characterized. The gene encoding the ...The key subunit II of cytochrome c oxidase (CcO) contains a soluble binuclear copper center (CuA) domain. The CUA domain of Paracoccus versutus was cloned, expressed, purified and characterized. The gene encoding the CUA domain in pETlld vector was expressed in E. coli BL21 (DE3). The results showed that the CuA domain was expressed mostly in inclusion bodies and the CUA domain protein synthesized in E. coli cells represents approximately 10 percent of the total cellular proteins. Dissolved in urea, dia-lyzed and recombined with Cu+/Cu2+ and purified by the Q-sepharose fast flow anion-exchange column and Sephadex G-75 gel filtration column, the soluble purple-colored protein, which shows a single band in electrophoresis, was obtained. The UV-visible absorption spectrum of CUA domain showed that there are intense band at 478 nm and a shoulder peak at 530 nm, and two weak bands at 360 and 806 nm respectively, which can be assigned to the charge transfer and the interactions of obitals of Cu-S and Cu-Cu展开更多
Kinetic studies of the heme dissociation from the wild type and Phe35Tyr, Phe35Leu mutants of bovine liver microsomal ferricytochrome b 5 indicate that the oxidized Phe35Tyr mutant is more stable towards denaturant th...Kinetic studies of the heme dissociation from the wild type and Phe35Tyr, Phe35Leu mutants of bovine liver microsomal ferricytochrome b 5 indicate that the oxidized Phe35Tyr mutant is more stable towards denaturant than wild type but Phe35Leu mutant proceeded with a different mechanism compared with wild type cytochrome b 5 and Phe35Tyr mutant protein. Because of the decrease of side chain volume in Phe35Leu mutant, a cavity produced in the interior of the protein may offer a channel for urea molecule to enter the hydrophobic pocket. When urea concentration is larger than 5 mol/L, the urea molecule may compete to coordinate the iron of heme with His39, that results in sharp increase of the rate of heme dissociation. The interaction between cytochrome b 5 and cytochrom c demonstrated that a 1:1 protein complex was formed between the two proteins. The binding constants of cytochrome b 5 with cytochrome c are: wild type K A=4.2(±0.01)×10 6(mol/L) -1 , Phe35Tyr K A=3.7(±0.01)×10 6(mol/L) -1 and Phe35Leu K A=4.7(±0.01)×10 6(mol/L) -1 respectively ( I =1 m mol/L, pH 7.0 soldium phosphate buffer, 25℃). These results clearly show that the mutation at Phe35 has no influence on the binding of cytochrome b 5 with cytochrome c and that the hydrophilic patch residues are not involved in the binding of cytochrome b 5 and cytochrome c.展开更多
基金the Continental Dynamics Program of the National Natural Science Foundation of China (Grant No. 40334041)the International Cooperation Program of the Ministry of Science and Technology of China (Grant No. 2003DF000011)Joint Seismological Science Foundation of China (Grant No.104060)
文摘The crustal and upper mantle azimuthal anisotropy of the Tibetan Plateau and adjacent areas was studied by Rayleigh wave tomography. We collected sufficient broadband digital seismograms trav-ersing the Tibetan Plateau and adjacent areas from available stations, including especially some data from the temporary stations newly deployed in Yunnan, eastern Tibet, and western Sichuan. They made an adequate path coverage in most regions to achieve a reasonable resolution for the inversion. The model resolution tests show that the anisotropic features of scope greater than 400 km and strength greater than 2% are reliable. The azimuthal anisotropy pattern inside the Tibetan Plateau was similar to the characteristic of tectonic partition. The crustal anisotropy strength is greater than 2% in most re-gions of East Tibet, and the anisotropy shows clockwise rotation surrounding the eastern Himalayan syntaxis. Vertically, the anisotropy direction indicates a coherent pattern within the upper crust, lower crust, and lithosphere mantle of the Tibetan Plateau, which also is consistent with GPS velocity field and SKS fast polarization directions. The result supports that the crust-mantle deformation beneath the Tibetan Plateau is vertically coherent. The anisotropy strength of crust and lithospheric upper mantle in Yunnan outside the Tibetan Plateau is lower than 2%, so SKS splitting from core-mantle boundary to station should largely be attributed to the anisotropy of asthenosphere.
基金This work was supported by the National Natural Science Foundation of China (Grant No. 39990600).
文摘The key subunit II of cytochrome c oxidase (CcO) contains a soluble binuclear copper center (CuA) domain. The CUA domain of Paracoccus versutus was cloned, expressed, purified and characterized. The gene encoding the CUA domain in pETlld vector was expressed in E. coli BL21 (DE3). The results showed that the CuA domain was expressed mostly in inclusion bodies and the CUA domain protein synthesized in E. coli cells represents approximately 10 percent of the total cellular proteins. Dissolved in urea, dia-lyzed and recombined with Cu+/Cu2+ and purified by the Q-sepharose fast flow anion-exchange column and Sephadex G-75 gel filtration column, the soluble purple-colored protein, which shows a single band in electrophoresis, was obtained. The UV-visible absorption spectrum of CUA domain showed that there are intense band at 478 nm and a shoulder peak at 530 nm, and two weak bands at 360 and 806 nm respectively, which can be assigned to the charge transfer and the interactions of obitals of Cu-S and Cu-Cu
文摘Kinetic studies of the heme dissociation from the wild type and Phe35Tyr, Phe35Leu mutants of bovine liver microsomal ferricytochrome b 5 indicate that the oxidized Phe35Tyr mutant is more stable towards denaturant than wild type but Phe35Leu mutant proceeded with a different mechanism compared with wild type cytochrome b 5 and Phe35Tyr mutant protein. Because of the decrease of side chain volume in Phe35Leu mutant, a cavity produced in the interior of the protein may offer a channel for urea molecule to enter the hydrophobic pocket. When urea concentration is larger than 5 mol/L, the urea molecule may compete to coordinate the iron of heme with His39, that results in sharp increase of the rate of heme dissociation. The interaction between cytochrome b 5 and cytochrom c demonstrated that a 1:1 protein complex was formed between the two proteins. The binding constants of cytochrome b 5 with cytochrome c are: wild type K A=4.2(±0.01)×10 6(mol/L) -1 , Phe35Tyr K A=3.7(±0.01)×10 6(mol/L) -1 and Phe35Leu K A=4.7(±0.01)×10 6(mol/L) -1 respectively ( I =1 m mol/L, pH 7.0 soldium phosphate buffer, 25℃). These results clearly show that the mutation at Phe35 has no influence on the binding of cytochrome b 5 with cytochrome c and that the hydrophilic patch residues are not involved in the binding of cytochrome b 5 and cytochrome c.
