锂离子电池正极材料LiFePO4的制备

对制备橄榄石型锂离子电池正极材料LiFePO4进行了实验研究,采用固相合成法合成了LiFePO4和掺杂碳的LiFePO4正极材料。分析测试结果表明:掺杂碳的LiFePO4作为正极材料具有良好的电化学性能,在0.1C倍率下放电,其室温初始放电容量为130mA·h/g,循环10次后几乎没有衰减。     

锂离子电池正极材料的研究现状

在简要介绍新一代充电电池——锂离子电池近年发展概况的基础上，阐述了锂离子电池几种正极材料（LiCoO2、LiNiO2、LiMn2O4、LiFePO4及锂钒氧化物等）的研究现状。     

锂离子电池正极材料研究动态

综述了近几年发展起来的一些锂离子电池正极材料，主要包括LiCoO2、LiNiO2、LiFePO4、LiMn2O4及锂钒氧化物等。重点介绍了锂锰氧化物的性能、制备及其改性等，并对纳米电极材料和其他正极材料的发展情况作了简要介绍。     

锂离子电池正极材料表面包覆的研究进展

锂离子电池正极材料是锂离子电池发展的关键。对锂离子电池正极材料进行包覆是改善其性能的有效方法。锂钴氧和锂锰氧正极材料表面包覆后的循环性能,特别是高温下的循环性能可以得到有效的改善。对于LiFePO4来讲,表面包覆主要是解决这类正极材料导电性问题。文章综述了国内外锂离子电池材料表面包覆的研究现状,提出了作者对将来研究方向的一些看法和建议。     

掺杂稀土的锂离子电池正极材料研究进展

锂离子电池由于高工作电压、高能量密度、低自放电率、长循环寿命等优点而被广泛应用于很多领域.本文综述了近几年来锂离子电池正极材料(LiCoO2、LiNiO2、LiMn2O4、LiFePO4)掺杂稀土的研究进展;着重叙述了用稀土修饰的LiCoO2和LiMn2O4的掺杂量、烧结工艺对正极材料结构和电化学性能的影响.简单介绍了用稀土修饰的LiNiO2和LiFePO4的结构和电化学性能.     

锂离子电池正极新材料LiFePO4的研究进展

高能量比、循环寿命长、成本低和无环境污染是目前锂离子电池正极材料的研究趋势.LiFePO4以其优良的电化学性能,被认为是最有前途的锂离子电池正极材料.该文综述了现有LiFePO4制备工艺,包括高温固相反应法、水热合成法、溶胶-凝胶法、微波合成法和改性法(如掺杂、包覆)等;并且指出LiFePO4可望于近期内在小功率电池中得到应用,而包覆、掺杂等改性手段是提高其电导率和粒子扩散速率的关键技术.     

锂离子电池正极材料LiFePO_4的研究进展

通过分析LiFePO4的橄榄石结构特点,介绍了近年来的各种制备方法及其改进途径,其中优化工艺、包覆和掺杂是提高材料性能的主要方法。认为LiFePO4目前还存在批次稳定性的产业化瓶颈,其作为动力型锂离子电池正极材料具有最广阔的应用前景。     

锂离子正极电池材料LiFePO4合成及改性的研究进展

橄榄石型结构的磷酸铁锂（LiFePO4）材料具有嵌入／脱出锂特性,对锂平台电压3．4V,理论比容量达170mA·h／g。该材料成本低廉,无毒性,对环境友好,充放电过程中能保持晶体结构的高度稳定,循环寿命长,耐高温性能好,可高倍率充放电,不会爆炸,是一种理想的锂离子二次电池正极材料。综述了LiFePO4电池正极材料的合成工艺与改性的研究进展。     

锂离子电池新型正极材料LiFePO4／C的合成

采用高温固相合成法合成了锂离子电池正极材料LiFePO4/C,并对其晶体结构、形貌和电化学性能进行了研究.结果表明:合成的LiFePO4/C材料为单一橄榄石型结构,颗粒分布比较均匀;以0.1 C倍率充放电时其初始比容量为115 mA·h/g,20次循环后其容量保持率为97%.     

微波法制备锂离子电池正极材料LiFePO4的研究

采用微波法制备锂离子电池正极材料LiFePO4，通过X射线衍射（XRD）、扫描电镜（SEM）、循环伏安和恒电流充放电测试等方法对材料的结构、表观形貌及电化学性能进行表征，考察了葡萄糖、导电碳黑等不同碳源对目标材料性能的影响。结果表明，采用微波法能快速简便地制备出均相LiFePO4；于0．1C倍率下，以葡萄糖作为碳源的正极材料首次放电比容量可达131．1mA·h／g，充放电30次循环后，容量损失率为2．1％；以导电炭黑作为碳源的正极材料首次放电比容量为118．3mA·h／g，充放电30次循环后，容量损失率为5．2％。     

共沉淀法制备锂离子电池正极材料LiFePO4

采用共沉淀法制备橄榄石结构的LiFePO4锂离子电池正极材料,通过X射线衍射(XRD)、透射电镜(TEM)、循环伏安(CV)和恒电流充放电测试等方法对其结构、表观形貌及电化学性能进行了分析研究.结果表明,该方法制备的LiFePO4为均一的橄榄石型晶体结构,颗粒微细;低倍率下充放电测试比容量可达126.3 mA·h/g;循环性能良好,充放电100次循环后,容量损失率仅为9.4%.     

Analysis of the factors affecting rate performance of LiFePO_4 lithium-ion batteries

In this paper,a water-based binder was used in LiFePO_4 Li-ion batteries and the factors affecting the battery performance were analyzed. The type and amount of conductive agent and the amount of binder were found to have a significant impact on the rate performance of LiFePO_4 Li-ion batteries. The impact of the two types of binders used in the test was not obvious.     

N236-HSCN体系萃取分离锆铪的盐效应研究

以乙酸戊酯作为稀释剂,采用N263-HSCN体系对锆、铪进行萃取分离,分别研究了(NH4)2SO4、NH4Cl、NH4NO3、NaCl和MgCl2等盐析剂的种类和浓度对锆与铪萃取分离的影响。结果表明,N263-HSCN体系分离锆、铪时优先萃取铪,该体系中SCN-的稳定性要比MIBK-HSCN体系强。不同阳离子的盐析剂对锆和铪的萃取率影响顺序为：NaCl>MgCl2>NH4Cl,对分离系数影响不大。不同阴离子的盐析剂对锆的萃取率顺序为：NH4NO3>NH4Cl>(NH4)2SO4,铪的萃取率顺序为：(NH4)2SO4>NH4Cl>NH4NO3,而分离系数顺序为：(NH4)2SO4>NH4Cl>NH4NO3,与阴离子的水合能力强弱顺序一致。当(NH4)2SO4加入量为0.6 mol/L时,分离系数达18.56,此时对锆和铪的萃取率分别为41.72%和93%。     

Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E

Human eukaryotic translation initiation factor 4E (eIF4E) binds to the mRNA cap structure and interacts with eIF4G, which serves as a scaffold protein for the assembly of eIF4E and eIF4A to form the eIF4F complex. eIF4E is an important modulator of cell growth and proliferation. It is the least abundant component of the translation initiation machinery and its activity is modulated by phosphorylation and interaction with eIF4E-binding proteins (4E-BPs). One strong candidate for the eIF4E kinase is the recently cloned MAPK-activated protein kinase, Mnk1, which phosphorylates eIF4E on its physiological site Ser209 in vitro. Here we report that Mnk1 is associated with the eIF4F complex via its interaction with the C-terminal region of eIF4G. Moreover, the phosphorylation of an eIF4E mutant lacking eIF4G-binding capability is severely impaired in cells. We propose a model whereby, in addition to its role in eIF4F assembly, eIF4G provides a docking site for Mnk1 to phosphorylate eIF4E. We also show that Mnk1 interacts with the C-terminal region of the translational inhibitor p97, an eIF4G-related protein that does not bind eIF4E, raising the possibility that p97 can block phosphorylation of eIF4E by sequestering Mnk1.     

Interactions of nucleotide release factor Dss4p with Sec4p in the post-Golgi secretory pathway of yeast

SEC4 is an essential gene encoding a small GTPase that is involved in Golgi to cell surface transport in Saccharomyces cerevisiae and is a paradigm for studies on the mode of action of Rab proteins. We describe here the features of interaction of Sec4p with the accessory protein Dss4p. Dss4p is found both on membranes and in the cytosol; however, it is the membrane fraction that is complexed to Sec4p. Dss4p, like its mammalian counterpart, Mss4, binds zinc, and disruption of the zinc-binding site disrupts the ability of the protein to interact with Sec4p. DSS4 overexpression can rescue the lethal phenotype of two alleles of SEC4, corresponding to dominant mutations of Ras. We demonstrate that this suppression is due to the ability of Dss4p to form a tight complex with the mutant forms of Sec4p and hence sequester the mutant protein from its inhibitory effect. These results imply an in vivo role for Dss4p as a guanine nucleotide dissociation stimulator. In vitro the protein has the ability to stimulate the dissociation rate of both GDP and GTP from Sec4p. We examined the relationship of GDI1 and DSS4 with SEC4 both genetically and biochemically. These results exclude a role for DSS4 in the recruitment of Sec4p/GDI onto membranes.     

Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein

eIF4E, the mRNA cap binding protein, is a master switch that controls eukaryotic translation. To be active, it must bind eIF4G and form the eIF4F complex, which also contains eIF4A. Translation is downregulated by association of eIF4E with 4E-BP, which occupies the eIF4G binding site. Signalling events acting on 4E-BP cause it to dissociate from eIF4E, and eIF4E is then free to bind eIF4G to form the active eIF4F complex. We have solved the structure of the yeast eIF4E/m7Gpp complex in a CHAPS micelle. We determined the position of the second nucleotide in a complex with m7GpppA, and identified the 4E-BP binding site. eIF4E has a curved eight-stranded antiparallel beta-sheet, decorated with three helices on the convex face and three smaller helices inserted in connecting loops. The m7G of the cap is intercalated into a stack of tryptophans in the concave face. The 4E-BP binding site is located in a region encompassing one edge of the beta-sheet, the adjacent helix a2 and several regions of non-regular secondary structure. It is adjacent to, but does not overlap the cap-binding site.     

Phosphorylation of tobacco eukaryotic translation initiation factor 4A upon pollen tube germination

Eukaryotic translation initiation factor eIF-4A is a member of the DEAD box family of RNA helicases and RNA-dependent ATPases. In tobacco, eIF-4A is encoded by a gene family with one isoform, eIF-4A8, being exclusively expressed in pollen. This pollen-specific isoform is a candidate for mediating translational control in the developing gametophyte. Here we show that eIF-4A is barely phosphorylated in mature pollen, but during pollen tube germination, two isoforms of eIF-4A become phosphorylated. Phosphoamino acid analysis indicated phosphorylation of threonine. In order to determine whether pollen-specific eIF-4A8 is among the phosphorylated isoforms, we raised transgenic tobacco plants overexpressing eIF-4A8 containing a histidine tag. Hereby, we could show that indeed eIF-4A8 is modified through phosphorylation. The biological relevance of the phosphorylation of eIF-4A is discussed.