汞、镉对土壤脲酶活性影响的研究Ⅰ.尿素浓度

对不同尿素浓度条件下重金属与土壤脲酶活性关系进行了研究。结果表明,尿素浓度对脲酶活性具有显著的影响。在供试浓度范围内可采用线性和Langmuir模型较好地表征二者关系。并得到脲酶活性的尿浓贡献率,尿浓贡献变化率和最大表观脲酶活性等参数;Hg,Cd明显降低了前述参数值,其中Hg Cd复合污染的抑制作用最强,Hg的生态毒性最大;同时初步获得土壤酶促反应过程中存在吸附机制。     

南瓜对镉的吸收积累特性研究

对南瓜进行盆栽试验,通过加入不同含量的镉、CaCO₃和草炭土,研究南瓜对镉的吸收积累特性,利用火焰原子吸收法测定。结果表明,南瓜植株对镉的富集量主要集中在茎、根中;当土壤镉含量小于5mg·kg^-1时,对南瓜根的生长有促进作用,当土壤镉含量大于5mg·kg^-1时,开始对根的生长产生抑制作用,抑制作用随镉含量的增大而加强;在土壤中施CaCO₃,能降低南瓜对镉的吸收;在土壤中加入草炭土,在一定范围内,它能促进南瓜对镉的吸收。     

芦苇抗镉污染机理研究

研究了芦苇幼苗体内 Cd的积累、亚细胞微区分布、存在形态和其诱导蛋白以及植物络合素合成抑制剂 (BSO)对芦苇光合作用和生长的影响。在 Cd污染条件下 ,芦苇幼苗植株和根皮层细胞中可积累大量的Cd,但 Cd在芦苇各器官和根皮层细胞亚细胞结构中的分布显著不均 ;Cd在芦苇幼苗体内的分配为 :根 >叶片 >茎 >地下茎 ,在根皮层细胞中的分布为 :细胞间隙 >细胞壁 >液泡 >细胞质。受 Cd污染的芦苇幼苗体内的 Cd以不同化学形态存在 ,其中 Na Cl提取态的 Cd在根和叶片中占的比例均为最大 ,其次为根内的醋酸提取态 ;在叶片中以水提取态为主 ,其它形态的含量相对较低。层析结果表明 ,根和叶片中各存在一种Cd结合蛋白 ,其中根内的 Cd结合蛋白可能是一种植物络合素聚合体。受 Cd诱导 ,芦苇幼苗根中还新合成了一种小分子蛋白或多肽 ,但另有一种蛋白因 Cd影响而消失。此外 ,BSO实验证明了植物络合素对 Cd的解毒作用。可见 ,芦苇的抗 Cd机理与以下几个方面有关 :根部截留 ,细胞间隙积累 ,细胞壁沉淀 ,液泡区域化 ,形成活性较低的难溶化合物 ,形成 Cd结合蛋白     

Proteomics reveals new insights into the role of light in cadmium response in Arabidopsis cell suspension cultures

Light plays an important role in plant growth, development, and response to environmental stresses. To investigate the effects of light on the plant responses to cadmium (Cd) stress, we performed a comparative physiological and proteomic analysis of light‐ and dark‐grown Arabidopsis cells after exposure to Cd. Treatment with different concentrations of Cd resulted in stress‐related phenotypes such as cell growth inhibition and decline of cell viability. Notably, light‐grown cells were more sensitive to heavy metal toxicity than dark‐grown cells, and the basis for this appears to be the elevated Cd accumulation, which is twice as much under light than dark growth conditions. Protein profiles analyzed by 2D DIGE revealed a total of 162 protein spots significantly changing in abundance in response to Cd under at least one of these two growing conditions. One hundred and ten of these differentially expressed protein spots were positively identified by MS/MS and they are involved in multiple cellular responses and metabolic pathways. Sulfur metabolism‐related proteins increased in relative abundance both in light‐ and dark‐grown cells after exposure to Cd. Proteins involved in carbohydrate metabolism, redox homeostasis, and anti‐oxidative processes were decreased both in light‐ and dark‐grown cells, with the decrease being lower in the latter case. Remarkably, proteins associated with cell wall biosynthesis, protein folding, and degradation showed a light‐dependent response to Cd stress, with the expression level increased in darkness but suppressed in light. The possible biological importance of these changes is discussed.     

Structural, molecular mechanics, and DFT study of cadmium(II) in its crown ether complexes with axially coordinated ligands, and of the binding of thiocyanate to cadmium(II)

The role of relativistic effects (RE) in the structures of Cd(II) complexes with crown ethers, and the reason the ‘soft’ Cd(II) strongly prefers to bind to SCN⁻ through N, are considered. The synthesis and structures of [Cd(18-crown-6)(thiourea)₂] (ClO₄)₂.18-crown-6 (1) and [Cd(Cy₂-18-crown-6)(NCS)₂] (2) are reported. (18-crown-6 = 1,4,7,10,13,16-hexaoxacyclooctadecane; Cy₂-18-crown-6 = cis-anti-cis-2,5,8,15,18,21-hexaoxatricylo[20.4.0.0(9,14)]hexacosane). In 1 Cd is coordinated in the plane of the crown which has close to D_3d symmetry, with long Cd-O bonds averaging 2.688 Å. The two thiourea molecules form relatively short Cd-S bonds that average 2.468 Å, with an S-Cd-S angle of 164.30°. This structure conforms with the idea that Cd(II) can adopt a near-linear structure involving two covalently-bound donor atoms (the S-donors) with short Cd-S bonds, which resembles gas-phase structures for species such as CdCl₂. The structure of 2 is similar, with the two SCN⁻ ligands N-bonded to Cd, with short Cd-N bonds of 2.106 Å, and N-Cd-N angle of 180°. The crown in 2 forms long Cd-O bonds that average 2.698 Å. Molecular mechanics calculations suggest that a main reason Cd(II) prefers to bind to SCN⁻ through N is that when bound through S, the small Cd-S-C angle, which is typically close to 100°, brings the ligand into close contact with other ligands present, and causes steric destabilization. In contrast, the Cd-N-C angles for SCN⁻ coordinated through N are much larger, being 171.4° in 2, which keeps the SCN⁻ groups well clear of the crown ether. DFT (density functional theory) calculations are used to generate the structures of [Cd(18-crown-6)(H₂O)₂]²⁺ (3) and [Cd(18-crown-6)Cl₂] (4). In 3, the Cd(II) is bound to only three O-donors of the macrocycle, with Cd-O bonds averaging 2.465 Å. The coordinated waters form an O-Cd-O angle of 139.47°, with Cd-O bonds of 2.295 Å. In contrast, for 4, the Cd is placed centrally in the cavity of the D_3d symmetry crown, with long Cd-O bonds averaging 2.906 Å. The Cl groups form a Cl-Cd-Cl angle of 180°, with short Cd-Cl bonds of 2.412 Å. With ionically bound groups on the axial sites of[Cd(18-crown-6)X₂] complexes, such as with X = H₂O in 3, the Cd(II) does not adopt linear geometry involving the two X groups, with long Cd-O bonds to the O-donors of the macrocycle. With covalently-bound X = Cl in 4, short Cd-Cl bonds and a linear [Cl-Cd-Cl] unit results, with long Cd-O bonds to the crown ether.     

Zinc(II) and cadmium(II) complexes based on 4-(3,5-diphenyl-1H-pyrazol-1-yl)-6-(piperidin-1-yl)pyrimidine (L): Synthesis, structure, luminescence. Double lone pair-π interactions in the structure of ZnL2Cl2

A series of zinc(II) and cadmium(II) complexes with 4-(3,5-diphenyl-1H-pyrazol-1-yl)-6-(piperidin-1-yl)pyrimidine (L), ZnLCl₂, CdLCl₂, ZnL₂Cl₂, CdL₂Cl₂, CdL₂Cl₂·0.5Me₂CO·1.5H₂O and CdL₂Cl₂·0.5CHCl₃·0.5H₂O, have been synthesized. The compounds ZnLCl₂ and CdLCl₂ were obtained in a M:L = 1:1 molar ratio in EtOH solutions, while ZnL₂Cl₂ and CdL₂Cl₂ were isolated in a M:L = 1:3 molar ratio in EtOH/Me₂CO mixtures. Surprisingly, attempts to crystallize CdLCl₂ from EtOH/Me₂CO mixture afforded single crystals of a compound, having 1:2 metal-to-ligand stoichiometry, CdL₂Cl₂·0.5Me₂CO·1.5H₂O, instead of a complex with 1:1 stoichiometry. At the same time, crystallization of CdL₂Cl₂ from Me₂CO/CHCl₃ mixture afforded CdL₂Cl₂·0.5CHCl₃·0.5H₂O single crystals. According to X-ray crystal structure data, ZnLCl₂, ZnL₂Cl₂, CdL₂Cl₂·0.5Me₂CO·1.5H₂O and CdL₂Cl₂·0.5CHCl₃·0.5H₂O complexes have molecular mononuclear structures. The molecules of L adopt bidentate chelating binding mode being coordinated to the metal ions through N² atom of the pyrazole and N³ atom of the pyrimidine rings. The coordination core of zinc atom in ZnLCl₂ complex is a distorted ZnN₂Cl₂ tetrahedron. The coordination cores of metal atoms in the structures of ZnL₂Cl₂, CdL₂Cl₂·0.5Me₂CO·1.5H₂O and CdL₂Cl₂·0.5CHCl₃·0.5H₂O are the distorted cis-MN₄Cl₂ (M = Zn, Cd) octahedra. In the structure of ZnL₂Cl₂ double lone pair(N(piperidine))-π(pyrimidine) interactions were observed. The photoluminescent properties of L, ZnLCl₂, CdLCl₂, ZnL₂Cl₂ and CdL₂Cl₂ were studied in the solid state under the same experimental conditions. These compounds were found to display bright blue luminescence. Highest relative intensity of emission was detected for ZnL₂Cl₂.     

Studies on the iodination of aras protein and the detection ofras polymers

Several methods for the iodination of recombinant v-H-ras protein were compared. The Iodobead method gave greates incorporation of radioactivity with minimal modification of theras protein. Upon treatment of theras protein with [¹²⁵I] Nal and an Iodobead, radioactivity was initially incorporated into a 22 kDa species with a pl of 5.2, then predominantly into a 23 kDa species with a pl of 5.4. The specific activity of [¹²⁵I]ras was 6×10⁶ cpm/pmol totalras protein. Iondination did not alter the biological activity of theras protein as judged by its ability to bind GTPS and induced maturation ofXenopus laevis oocytes. It is concluded that while iodination alters the apparent molecular weight and pI ofras, presumably by the oxidation of one or more classes of amino acids, this does not affect the biological function of the protein. Theras protein, radioactively-labelled with iodine using the Iodobead method, should be suitable for studies of protein-protein interactions involvingras. Treatment of iodinatedras with the chemical cross-linking agent disuccinimidyl suberate revealed the presence of several minor high molecular weight protein species. This result shows that, in a dilute solution of purifiedras protein, the monomeric form is in equilibrium with small amounts of polymeric forms.Abbreviations DSS Disuccinimidyl Suberate - GTPS Guanosine 5-[-thio] triphosphate - ATPS Adenosine 5[-thio] Triphosphate     

镉在有机酸存在时对红壤中微生物生物量的影响

在预培红壤中加入定量的有机酸和不同浓度的Cd ,2 5℃培养 14d ,测定土壤微生物生物量C(Cmic)、N(Nmic) ,结果表明 ,存在有机酸时 ,土壤中Cmic和Nmic随着Cd浓度的增加而降低 ;Cmic/Nmic随着Cd浓度的增加而升高 .施加低分子量有机酸的土壤中 ,Cd浓度高于 2 5mg·kg-1土时 ,土壤中Cmic和Nmic均比未加有机酸时低 ,说明此时低分子量有机酸助长Cd的毒性 ,而Cd浓度低于 2 5mg·kg-1土时 ,土壤中Cmic和Nmic均比未加有机酸时高 ,说明此时低分子量有机酸可降低部分Cd的毒性 ;施加胡敏酸的土壤中 ,土壤中Cmic和Nmic均比未加有机酸时高 ,说明胡敏酸降低Cd的毒性并提供N源 .不含Cd时 ,加入有机酸导致土壤中Cmic和Nmic增加 ,其中胡敏酸最明显     

Horse heart ferricytochrome c: conformation and heme configuration of low ionic strength acidic forms

Resonance Raman, absorption and circular dichroism spectroscopic studies of the stable forms of horse heart ferricytochromec in thepH range 6–0.8 and at the lowest possible ionic strengths, in water, and at 30°C are reported. The neutralpH form, state III, changes to the acidicpH form, state I, through a three-step process: state III state IIIa state II state I, with pKa's of 3.6±0.3, 2.7±0.2, and 1.2±0.2, depending on the monitoring probe, respectively. State IIIa ferricytochromec is like state III (i.e., with the Met-80-sulfur-iron linkage and a closed heme crevice) but with a higher degree of folding and a slightly larger porphyrin core. State II ferricytochromec is an unfolded form with an open heme crevice and no Met-80-sulfur-iron linkage. The heme iron is high-spin and hexacoordinated with weak ligand-field groups, water, and nitrogen of the protonated/hydrogen-bonded imidazole of the His-18 residue at the axial positions. The state I form also lacks the Met-80-sulfur-iron linkage and has an open heme crevice like the state II form; however, it is less unfolded and has a high-spin pentacoordinated heme iron, with the nitrogen of the imidazole of His-18 as the axial ligate, which is out of the porphyrin plane by about 0.45 Å.