Density functional theory study with and without COSMO of H2 SO4 reactions in an aqueous environment for metal extraction.

In a recent study investigating the suitability of solvent extraction (SX) for the separation of Ta and Nb, it was shown that speciation data would be required to help explain the data obtained. As traditional speciation techniques cannot be readily applied for Ta and Nb, it was decided to determine the suitability of molecular modeling for this purpose. During the SX experiments the aqueous phase consisted of sulfuric acid (H2 SO4 ), water, and metal species. In this study density functional theory (DFT) modeling was used to calculate the formation energy of five possible reactions of H2 SO4 and H2 O. Different functional and basis set combinations were compared as well as the effect of infinite dilution by using the conductor-like screening model (COSMO), which simulates infinite dilution of solvents of varying polarity and includes the short-range interactions of the solute particles. The results obtained were used to determine whether it is possible to predict the reactions and mechanism when H2 SO4 and H2 O interact during SX. According to the results, the deprotonation of H2 SO4 was endothermic in a 1:1 acid-water ratio, while being both exothermic in the 1:5 and 1:10 acid-water ratio forming HSO4 - and SO4 2- respectively. Furthermore, it was seen that the hydration and dehydration of H2 SO4 in a bulk H2 O solution was a continuous process. From the energy calculations it was determined that although the H2 SO4 ●H2 O, HSO4 - ●H2 O, and H2 SO4 ●2H2 O species could form, they would most likely react with H2 O molecules to form HSO4 - , H3 O+ , and H2 O. © 2018 Wiley Periodicals, Inc.

Identification of peptide metabolites of Microcystis (Cyanobacteria) that inhibit trypsin-like activity in planktonic herbivorous Daphnia (Cladocera).

Cyanobacteria are recognized as producers of a broad variety of bioactive metabolites. Among these, the peptides synthesized by the non-ribosomal peptide synthetase pathway occur in high structural variability. One class of cyanobacterial peptides, the cyanopeptolins or micropeptins, have been shown to be strong inhibitors of vertebrate serine proteases, like trypsin. In the present study we screened extracts of ten strains of the unicellular cyanobacterium Microcystis sp. for their potential to inhibit trypsin-like activity in the planktonic crustacea Daphnia, the main herbivores in freshwater ecosystem. Respective standardized IC(50)'s varied for nearly two orders of magnitude. In HPLC fractions we could identify mainly cyanopeptolins as active compounds by MALDI-TOF mass spectrometry. Cyanopeptolins were found in 22 structural variants with 13 variants produced by one strain alone. Peptides of the microviridin class were moderately active while no activity was evident for microginins and microcystins. Among the cyanopeptolins only those were active that had an arginine or lysine residue N-terminal to the modified amino acid 3-amino-6-hydroxy-piperidone. Structural variants that had a tyrosine residue at this particular position did not inhibit trypsin-like activity. The highly variable composition of the side chain of cyanopeptolins had no marked effect on the activity. Among the six cyanobacterial strains we tested intensively two did not produce any cyanopeptolins and were accordingly less active as crude extracts. The present study underlines the potential importance of the biochemistry of cyanobacteria for the feeding ecology of a planktonic herbivore.

Isolation, characterization, and quantitative analysis of Microviridin J, a new Microcystis metabolite toxic to Daphnia.

This paper describes the purification and characterization of microviridin J. a newly discovered metabolite of Microcystis that causes a lethal molting disruption in Daphnia spp., upon ingestion of living cyanobacterial cells. Microviridin J consists of an acetylated chain of 13 amino acids arranged in three rings and two side chains. Unlike other known isoforms of microviridin, microviridin J contains arginine that imparts a unique solution conformation characterized by proximal hydrophobic interactions between Arg and other regions of the molecule. This eventually results in the formation and stabilization of an additional ring system. Microviridin J potently inhibits porcine trypsin, bovine chymotrypsin, and daphnid trypsin-like proteases. The activity against trypsin is most likely due to Arg and its distinctive conformational interactions. Overall, the data presented for microviridin J emphasize once again the ability of cyanobacteria to produce numerous and potent environmental toxins.