Kinetics and Adsorption Isotherms of Bisphenol A, Estrone, 17 beta-Estradiol, and 17 alpha-Ethinylestradiol in Tropical Sediment Samples

The sorption of four endocrine disruptors, bisphenol A (BPA), estrone (E1), 17 beta-estradiol (E2), and 17 alpha-ethinylestradiol (EE2) in tropical sediment samples was studied in batch mode under different conditions of pH, time, and sediment amount. Data obtained from sorption experiments using the endocrine disruptors (EDs) and sediments containing different amounts of organic matter showed that there was a greater interaction between the EDs and organic matter (OM) present in the sediment, particularly at lower pH values. The pseudosecond order kinetics model successfully explained the interaction between the EDs and the sediment samples. The theoretical and experimentally obtained q (e) values were similar, and k values were smaller for higher SOM contents. The k (F) values, obtained from the Freundlich isotherms, varied in the ranges 4.2-7.4 x 10(-2) (higher OM sediment sample, S(2)) and 1.7 x 10(-3)-3.1 x 10(-2) (lower OM sediment sample, S(1)), the latter case indicating an interaction with the sediment that increased in the order: EE2 > > E2 > E1 > BPA. These results demonstrate that the availability of endocrine disruptors may be directly related to the presence of organic material in sediment samples. Studies of this kind provide an important means of understanding the mobility, transport, and/or reactivity of this type of emergent contaminant in aquatic systems.

Structural and Biochemical Characterization of Peroxiredoxin Q beta from Xylella fastidiosa CATALYTIC MECHANISM and HIGH REACTIVITY

The phytopathogenic bacterium Xylella fastidiosa is the etiological agent of various plant diseases. To survive under oxidative stress imposed by the host, microorganisms express antioxidant proteins, including cysteine-based peroxidases named peroxiredoxins. This work is a comprehensive analysis of the catalysis performed by PrxQ from X. fastidiosa (XfPrxQ) that belongs to a peroxiredoxin class still poorly characterized and previously considered as moderately reactive toward hydroperoxides. Contrary to these assumptions, our competitive kinetics studies have shown that the second-order rate constants of the peroxidase reactions of XfPrxQ with hydrogen peroxide and peroxynitrite are in the order of 107 and 106 M(-1) s(-1), respectively, which are as fast as the most efficient peroxidases. The XfPrxQ disulfides were only slightly reducible by dithiothreitol; therefore, the identification of a thioredoxin system as the probable biological reductant of XfPrxQ was a relevant finding. We also showed by site-specific mutagenesis and mass spectrometry that an intramolecular disulfide bond between Cys-47 and Cys-83 is generated during the catalytic cycle. Furthermore, we elucidated the crystal structure of XfPrxQ C47S in which Ser-47 and Cys-83 lie similar to 12.3 angstrom apart. Therefore, significant conformational changes are required for disulfide bond formation. In fact, circular dichroism data indicated that there was a significant redox-dependent unfolding of alpha-helices, which is probably triggered by the peroxidatic cysteine oxidation. Finally, we proposed a model that takes data from this work as well data as from the literature into account.