Vanadium trioxide（V2O3） was directly prepared by NaVO3 electrolysis in Na Cl molten salts. Electrolysis products were characterized by X-ray diffraction（XRD）, scanning electron microscopy（SEM） and energy dispers...Vanadium trioxide（V2O3） was directly prepared by NaVO3 electrolysis in Na Cl molten salts. Electrolysis products were characterized by X-ray diffraction（XRD）, scanning electron microscopy（SEM） and energy dispersive spectroscopy（EDS）. The existing state and electrochemical behavior of NaVO3 were also studied. The results indicated that V2O3 can be obtained from NaVO3. VC and C were also formed at high cell voltage, high temperature, and long electrolysis time. During electrolysis, NaVO3 was dissociated to Na＋ and VO3-in Na Cl molten salt. NaVO3 was initially electro-reduced to V2O3 on cathode and Na2O was released simultaneously. Na2CO3 was formed due to the reaction between Na2O and CO2. The production of C was ascribed to the electro-reduction of CO3（2-）. VC was produced due to the reaction between C and V2O3.展开更多
研究了在氧气存在下生物质催化氧化制甲酸体系中甲酸的稳定性,主要考察了反应温度、反应时间、氧气初始压力、硫酸浓度、催化剂等因素对于甲酸分解的影响。研究结果表明,温度、反应时间、硫酸浓度对甲酸的分解速率有显著的影响;氧气的...研究了在氧气存在下生物质催化氧化制甲酸体系中甲酸的稳定性,主要考察了反应温度、反应时间、氧气初始压力、硫酸浓度、催化剂等因素对于甲酸分解的影响。研究结果表明,温度、反应时间、硫酸浓度对甲酸的分解速率有显著的影响;氧气的初始压力对于甲酸的分解影响较小;催化剂NaVO3的存在会加速甲酸的分解。生物质催化氧化体系中,甲酸的分解反应为二级反应,甲酸分解反应的表观活化能为85.1 k J/mol。提出了在H2SO4溶液中氧气气氛下NaVO3催化甲酸分解的机理。展开更多
Water deficit-induced ABA accumulation is an ideal model or 搒timulus-response?system to investigate cellular stress signaling in plant cells, using such a model the cellular stress signaling triggered by water defici...Water deficit-induced ABA accumulation is an ideal model or 搒timulus-response?system to investigate cellular stress signaling in plant cells, using such a model the cellular stress signaling triggered by water deficit was inves-tigated in Maize L. coleoptile. Water deficit-induced ABA accumulation was sensitively blocked by NaVO3, a potent inhibitor both to plasma membrane H+-ATPase (PM-H+- ATPase) and protein tyrosine phosphatase (PTPase). How-ever, while PM- H+-ATPase activity was unaffected under water deficit and PM- H+-ATPase activator did not induce an ABA accumulation instead of water deficit, water deficit induced an increase in the protein phosphatase activity, and furthermore, ABA accumulation was inhibited by PAO, a specific inhibitor of PTPase. These results indicate that pro-tein phosphtases may be involved in the cellular signaling in response to water deficit. Further studies identified at least four species of protein phosphtase as assayed by using pNPP as substrate, among which one component was especially sensitive to NaVO3. The NaVO3-sensitive enzyme was puri-fied and finally showed a protein band about 66 kD on SDS/PAGE. The purified enzyme showed a great activity to some specific PTPase substrates at pH 6.0. In addition to NaVO3, the enzyme was also sensitive to some other PTPase inhibitors such as Zn2+ and MO33+, but not to Ca2+ and Mg2+, indicating that it might be a protein tyrosine phosphatase. Interestingly, the purified enzyme could be deactivated by some reducing agent DTT, which was previously proved to be an inhibitor of water deficit-induced ABA accumulation. This result further proved that PTPase might be involved in the cellular signaling of ABA accumulation in response to water deficit.展开更多
基金supported by the National Basic Research Program of China(973 Program)(No.2013CB632606)National Natural Science Foundation of China(Nos.51474200,51422405)Youth Innovation Promotion Association,CAS(No.2015036)
文摘Vanadium trioxide（V2O3） was directly prepared by NaVO3 electrolysis in Na Cl molten salts. Electrolysis products were characterized by X-ray diffraction（XRD）, scanning electron microscopy（SEM） and energy dispersive spectroscopy（EDS）. The existing state and electrochemical behavior of NaVO3 were also studied. The results indicated that V2O3 can be obtained from NaVO3. VC and C were also formed at high cell voltage, high temperature, and long electrolysis time. During electrolysis, NaVO3 was dissociated to Na＋ and VO3-in Na Cl molten salt. NaVO3 was initially electro-reduced to V2O3 on cathode and Na2O was released simultaneously. Na2CO3 was formed due to the reaction between Na2O and CO2. The production of C was ascribed to the electro-reduction of CO3（2-）. VC was produced due to the reaction between C and V2O3.
文摘研究了在氧气存在下生物质催化氧化制甲酸体系中甲酸的稳定性,主要考察了反应温度、反应时间、氧气初始压力、硫酸浓度、催化剂等因素对于甲酸分解的影响。研究结果表明,温度、反应时间、硫酸浓度对甲酸的分解速率有显著的影响;氧气的初始压力对于甲酸的分解影响较小;催化剂NaVO3的存在会加速甲酸的分解。生物质催化氧化体系中,甲酸的分解反应为二级反应,甲酸分解反应的表观活化能为85.1 k J/mol。提出了在H2SO4溶液中氧气气氛下NaVO3催化甲酸分解的机理。
基金the National Natural Science Foundation of China (Grant Nos.30070071& 30270135)and the National Key Basic Research Project (Grant No. G1999011700)
文摘Water deficit-induced ABA accumulation is an ideal model or 搒timulus-response?system to investigate cellular stress signaling in plant cells, using such a model the cellular stress signaling triggered by water deficit was inves-tigated in Maize L. coleoptile. Water deficit-induced ABA accumulation was sensitively blocked by NaVO3, a potent inhibitor both to plasma membrane H+-ATPase (PM-H+- ATPase) and protein tyrosine phosphatase (PTPase). How-ever, while PM- H+-ATPase activity was unaffected under water deficit and PM- H+-ATPase activator did not induce an ABA accumulation instead of water deficit, water deficit induced an increase in the protein phosphatase activity, and furthermore, ABA accumulation was inhibited by PAO, a specific inhibitor of PTPase. These results indicate that pro-tein phosphtases may be involved in the cellular signaling in response to water deficit. Further studies identified at least four species of protein phosphtase as assayed by using pNPP as substrate, among which one component was especially sensitive to NaVO3. The NaVO3-sensitive enzyme was puri-fied and finally showed a protein band about 66 kD on SDS/PAGE. The purified enzyme showed a great activity to some specific PTPase substrates at pH 6.0. In addition to NaVO3, the enzyme was also sensitive to some other PTPase inhibitors such as Zn2+ and MO33+, but not to Ca2+ and Mg2+, indicating that it might be a protein tyrosine phosphatase. Interestingly, the purified enzyme could be deactivated by some reducing agent DTT, which was previously proved to be an inhibitor of water deficit-induced ABA accumulation. This result further proved that PTPase might be involved in the cellular signaling of ABA accumulation in response to water deficit.
