在本研究中,提出了一种简单快速的衍生化和预富集方法,称为涡旋辅助分散液-液微萃取(VA-DLLME),用于在形成其挥发性衍生物后通过气相色谱-质谱法(GC-MS)测定硒。与o-湖水样品中的苯二胺 (Se-PDA-FVD)。通过实施开发的衍生化程序,利用气相色谱系统来测定无机硒。采用 VA-DLLME 方法通过预浓缩分析物来增强 GC-MS 系统的检测能力。优化衍生化和萃取程序变量,包括缓冲溶液的 pH 值和体积、衍生剂的体积、混合的类型和时间段、分散剂和萃取溶剂的类型/体积,以提高萃取产量。在最佳衍生/预富集条件下,测定了VA-DLLME-Se-PDA-FVD-GC-MS方法的分析性能。检测限 (LOD) 和定量限 (LOQ) 计算为 2.2 ng mL -1分别为7.3 ng mL -1 和7.3 ng mL -1。用湖水进行加标实验,以检验该方法的准确性和适用性。加标样品的回收率结果在
all other cases of substrate reduction by oxo transfer, the kinetic metal effect k(2)W > k(2)Mo holds. A proposal from primary sequence alignments suggesting that a conserved Asp residue is a likely ligand in the type II enzymes in the DMSO reductase family has been pursued by synthesis of the [Mo(IV)(O2CR)(S2C2Me2)2](1-) (R = Ph, Bu(t)) complexes. The species display symmetrical eta2-carboxylate binding
Although there has been no report on the catalytic reaction of selenate over heterogeneous catalysts in aqueous solution, we found that titania-supported Pt catalysts exhibited significantly high activity for the reduction of selenate with hydrazine. The Pt catalysts were deactivated during the reaction because of the deposition of Se metal, but showed excellent reusability. Therefore, it was firstly demonstrated that heterogeneous catalysts are effective for the removal of selenate from aqueous solution.
Oxyanions of arsenic and selenium can be used in microbial anaerobic respiration as terminal electron acceptors. The detection of arsenate and selenate respiring bacteria in numerous pristine and contaminated environments and their rapid appearance in enrichment culture suggest that they are widespread and metabolically active in nature. Although the bacterial species that have been isolated and characterized are still few in number, they are scattered throughout the bacterial domain and include Gram-positive bacteria, beta, gamma and epsilon Proteobacteria and the sole member of a deeply branching lineage of the bacteria, Chrysiogenes arsenatus. The oxidation of a number of organic substrates (i.e. acetate, lactate, pyruvate, glycerol, ethanol) or hydrogen can be coupled to the reduction of arsenate and selenate, but the actual donor used varies from species to species. Both periplasmic and membrane-associated arsenate and selenate reductases have been characterized. Although the number of subunits and molecular masses differs, they all contain molybdenum. The extent of the environmental impact on the transformation and mobilization of arsenic and selenium by microbial dissimilatory processes is only now being fully appreciated.
Selenium oxyanions, particularly selenite, can be highly toxic to living organisms. Few bacteria reduce both selenate and selenite into the less toxic elemental selenium. Insights into the mechanisms of the transport and the reduction of selenium oxyanions in Escherichia coli were provided by a genetic analysis based on transposon mutagenesis. Ten mutants impaired in selenate reduction were analysed. Three of them were altered in genes encoding transport proteins including a porin, an inner-membrane protein and a sulfate carrier. Two mutants were altered in genes required for molybdopterin biosynthesis, strongly suggesting that the selenate reductase of E. coli is a molybdoenzyme. However, mutants deleted in various oxomolybdenum enzymes described so far in this species still reduced selenate. Finally, a mutant in the gene ygfK encoding a putative oxidoreductase was obtained. This gene is located upstream of ygfN and ygfM in the ygfKLMN putative operon. YgfN and YgfM code for a molybdopterin-containing enzyme and a polypeptide carrying a FAD domain, respectively. It is therefore proposed that the selenate reductase of E. coli is a structural complex including the proteins YgfK, YgfM and YgfN. In addition, all the various mutants were still able to reduce selenite into elemental selenium. This implies that the transport and reduction of this compound are clearly distinct from those of selenate.