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51.
52.
A Pseudomonas isolate, designated PAHAs-1, was found capable of reducing arsenate and degrading polycyclic aromatic hydrocarbons (PAHs) independently and simultaneously. This isolate completely reduced 1.5 mM arsenate within 48 h and removed approximately 100% and 50% of 60 mg l−1 phenanthrene and 20 mg l−1 pyrene within 60 h, respectively. Using PAHs as the sole carbon source, however, this isolate showed a slow arsenate reduction rate (4.62 μM h−1). The presence of arsenic affected cell growth and concurrent PAHs removal, depending on PAH species and arsenic concentration. Adding sodium lactate to the medium greatly enhanced the arsenate reduction and pyrene metabolism. The presence of the alpha subunit of the aromatic ring-hydroxylating dioxygenase (ARHD) gene, arsenate reductase (arsC) and arsenite transporter (ACR3(2)) genes supported the dual function of the isolate. The finding of latter two genes indicated that PAHAs-1 possibly reduced arsenate via the known detoxification mechanism. Preliminary data from hydroponic experiment showed that PAHAs-1 degraded the majority of phenanthrene (>60%) and enhanced arsenic uptake by Pteris vittata L. (from 246.7 to 1187.4 mg kg−1 As in the fronds). The versatile isolate PAHAs-1 may have potentials in improving the bioremediation of PAHs and arsenic co-contamination using the plant-microbe integrated strategy. 相似文献
53.
(1) Rates of ATP synthesis and ADP-arsenate synthesis catalyzed by Rhodospirillum rubrum chromatophores were determined with the firefly luciferase method and by a coupled enzyme assay involving hexokinase and glucose-6-phosphate dehydrogenase. (2) Vm for ADP-arsenate synthesis was about 2-times lower than Vm for ATP-synthesis. With saturating [ADP], K(Asi) was about 20% higher than K(Pi). With saturating [anion], K(ADP) was during arsenylation about 20% lower than during phosphorylation. (3) Plots of vs. were non-linear at low concentrations of the fixed substrate. The non-linearity was such as to suggest a positive cooperativity between sites binding the variable substrate, resulting in an increased ratio. High concentrations of the fixed substrate cause a similar increase in , but abolish the cooperativity of the sites binding the variable substrate. (4) Low concentrations of inorganic arsenate (Asi) stimulate ATP synthesis supported by low concentrations of Pi and ADP about 2-fold. (5) At high ADP concentrations, the apparent Ki of Asi for inhibition of ATP-synthesis was 2–3-times higher than the apparent Km of Asi for arsenylation; the apparent Ki of Pi for inhibition of ADP-arsenate synthesis was about 40% lower than the apparent Km of Pi for ATP synthesis. (6) The results are discussed in terms of a model in which Pi and Asi compete for binding to a catalytic as well as an allosteric site. The interaction between these sites is modulated by the ADP concentration. At high ADP concentrations, interaction between these sites occurs only when they are occupied with different species of anion. 相似文献