The role of arbuscular mycorrhiza and organosulfur mobilizing bacteria in plant sulphur supply

AM fungi are enhancing growth and health of many land plants but only some of these beneficial mechanisms are well understood. This study aimed to uncover the role of bacteria colonising AM fungi in organically-bound sulfur (S) mobilisation, the dominant S pools in soil that are not directly available to plants. The effect of an intact AM symbiosis with access to stable isotope organo-34S enriched soils encased in 35 µm mesh cores was tested in microcosms with Agrostis stolonifera and Plantago lanceolata. At 3 month intervals, the plant shoots were analysed for 34S uptake. After 9 months, hyphae and associated soil was picked from static (mycorrhizal) and rotating (severed hyphae) mesh cores and corresponding rhizosphere soil was sampled for bacterial analysis. AM symbiosis increased uptake of 34S from organo-34S enriched soil at early stages of plant growth when S demand appeared to be high. The static (mycorrhizal) treatments were shown to harbour larger populations of cultivable heterotrophs and sulfonate mobilising bacteria. Microbial communities were significantly different in the hyphosphere of mycorrhizal hyphae and hyphae not associated to plant hosts. Sulfate ester (arylsulfatase enzyme assay, atsA gene) and sulfonate mobilising activity (asfA gene) was altered by an intact AM symbiotic partnership which stimulated the genera Azospirillum, Burkholderia and Polaromonas. Illumina sequencing revealed that AM symbiosis led to community shifts, reduced diversity and dominance of the Planctomycetes and Proteobacteria. This study demonstrated that AM symbioses can promote organo-S mobilization and plant uptake through interaction with hyphospheric bacteria.Research highlightsAM hyphae enhanced uptake of organically bound 34S at early stages of growth.AM hyphosphere harboured a large population of organo-S desulfurizing bacteria.Microbial communities significantly differed in rotating and static mesh cores.AM hyphae influenced bacterial sulfate ester and sulfonate mobilising activity.AM hyphae reduced bacterial diversity, increased Planctomycetes and Proteobacteria abundance.

Modeling the Alkaline Hydrolysis of Diaryl Sulfate Diesters: A Mechanistic Study

<div> <div> <div> <p>Phosphate and sulfate esters have important roles as biological building blocks and in regulating cellular processes. However, while there has been substantial experimental and computational investigation of the mechanisms and the transition states involved in phosphate ester hydrolysis, there is far less (in particular computational) work on sulfate ester hydrolysis. Here, we report a detailed computational study of the alkaline hydrolysis of diaryl sulfate diesters, using different DFT functionals and both pure implicit solvation as well as mixed implicit/explicit solvation with varying numbers of explicit water molecules. We consider both the impact of how the system is modeled on computed linear free energy relationships (LFER) and the nature of the transition states. Although our calculations consistently underestimate the absolute activation free energies, we obtain good agreement with experimental LFER data when using pure implicit solvent, and excellent agreement with experimental kinetic isotope effects for all models used. Our calculations suggest that the hydrolysis of sulfate diesters proceeds through loose transition states, with minimal bond formation to the nucleophile and with bond cleavage to the leaving group already initiated. Comparison to prior work indicates that these transition states are similar in nature to those of analogous reactions such as the alkaline hydrolysis of neutral arylsulfonate monoesters or charged phosphate diesters and fluorophosphates. Obtaining more detailed insight into the transition states involved assists in understanding the selectivity of enzymes that hydrolyze these reactions; however, this work also highlights the methodological challenges involved in reliably modeling sulfate ester hydrolysis. </p> </div> </div> </div>

Modeling the Alkaline Hydrolysis of Diaryl Sulfate Diesters: A Mechanistic Study

<div> <div> <div> <p>Phosphate and sulfate esters have important roles as biological building blocks and in regulating cellular processes. However, while there has been substantial experimental and computational investigation of the mechanisms and the transition states involved in phosphate ester hydrolysis, there is far less (in particular computational) work on sulfate ester hydrolysis. Here, we report a detailed computational study of the alkaline hydrolysis of diaryl sulfate diesters, using different DFT functionals and both pure implicit solvation as well as mixed implicit/explicit solvation with varying numbers of explicit water molecules. We consider both the impact of how the system is modeled on computed linear free energy relationships (LFER) and the nature of the transition states. Although our calculations consistently underestimate the absolute activation free energies, we obtain good agreement with experimental LFER data when using pure implicit solvent, and excellent agreement with experimental kinetic isotope effects for all models used. Our calculations suggest that the hydrolysis of sulfate diesters proceeds through loose transition states, with minimal bond formation to the nucleophile and with bond cleavage to the leaving group already initiated. Comparison to prior work indicates that these transition states are similar in nature to those of analogous reactions such as the alkaline hydrolysis of neutral arylsulfonate monoesters or charged phosphate diesters and fluorophosphates. Obtaining more detailed insight into the transition states involved assists in understanding the selectivity of enzymes that hydrolyze these reactions; however, this work also highlights the methodological challenges involved in reliably modeling sulfate ester hydrolysis. </p> </div> </div> </div>

Green Production of Potassium Sulfate by Hydrothermal Carbonization of Carrageenan

A novel green method of producing potassium sulfate from a sustainable source is described. Aqueous carrageenan is subjected to hydrothermal carbonization inside a pressure vessel. Separation of the liquid component from the hydrochar followed by evaporation to dryness and treatment with ethanol afforded potassium sulfate. Characterization using SEM-EDX, XRD and Raman spectroscopy confirms the identity of potassium sulfate in the form of K3H(SO4)2. The green process allows the facile release of sulfate ester group from the carrageenan chains and combining with the residual potassium ions in the carrageenan. The new method allows for the simplification of the process of producing potassium sulfate in an environmental friendly way and using a renewable source.

Sulfate Ester Detergent Degradation in Pseudomonas aeruginosa Is Subject to both Positive and Negative Regulation

ABSTRACT Bacteria using toxic chemicals, such as detergents, as growth substrates face the challenge of exposing themselves to cell-damaging effects that require protection mechanisms, which demand energy delivered from catabolism of the toxic compound. Thus, adaptations are necessary for ensuring the rapid onset of substrate degradation and the integrity of the cells. Pseudomonas aeruginosa strain PAO1 can use the toxic detergent sodium dodecyl sulfate (SDS) as a growth substrate and employs, among others, cell aggregation as a protection mechanism. The degradation itself is also a protection mechanism and has to be rapidly induced upon contact to SDS. In this study, gene regulation of the enzymes initiating SDS degradation in strain PAO1 was studied. The gene and an atypical DNA-binding site of the LysR-type regulator SdsB1 were identified and shown to activate expression of the alkylsulfatase SdsA1 initiating SDS degradation. Further degradation of the resulting 1-dodecanol is catalyzed by enzymes encoded by laoCBA, which were shown to form an operon. Expression of this operon is regulated by the TetR-type repressor LaoR. Studies with purified LaoR identified its DNA-binding site and 1-dodecanoyl coenzyme A as the ligand causing detachment of LaoR from the DNA. Transcriptional studies revealed that the sulfate ester detergent sodium lauryl ether sulfate (SLES) induced expression of sdsA1 and the lao operon. Growth experiments revealed an essential involvement of the alkylsulfatase SdsA1 for SLES degradation. This study revealed that the genes for the enzymes initiating the degradation of toxic sulfate-ester detergents are induced stepwise by a positive and a negative regulator in P. aeruginosa strain PAO1. IMPORTANCE Bacterial degradation of toxic compounds is important not only for bioremediation but also for the colonization of hostile anthropogenic environments in which biocides are being used. This study with Pseudomonas aeruginosa expands our knowledge of gene regulation of the enzymes initiating degradation of sulfate ester detergents, which occurs in many hygiene and household products and, consequently, also in wastewater. As an opportunistic pathogen, P. aeruginosa causes severe hygienic problems because of its pronounced biocide resistance and its metabolic versatility, often combined with its pronounced biofilm formation. Knowledge about the regulation of detergent degradation, especially regarding the ligands of DNA-binding regulators, may lead to the rational development of specific inhibitors for restricting growth and biofilm formation of P. aeruginosa in hygienic settings. In addition, it may also contribute to optimizing bioremediation strategies not only for detergents but also for alkanes, which when degraded merge with sulfate ester degradation at the level of long-chain alcohols.

Heterogeneous OH oxidation of isoprene-epoxydiol-derived organosulfates: kinetics, chemistry and formation of inorganic sulfate

Acid-catalyzed multiphase chemistry of epoxydiols formed from isoprene oxidation yields the most abundant organosulfates (i.e., methyltetrol sulfates) detected in atmospheric fine aerosols in the boundary layer. This potentially determines the physicochemical properties of fine aerosols in isoprene-rich regions. However, chemical stability of these organosulfates remains unclear. As a result, we investigate the heterogeneous oxidation of aerosols consisting of potassium 3-methyltetrol sulfate ester (C5H11SO7K) by gas-phase hydroxyl (OH) radicals at a relative humidity (RH) of 70.8 %. Real-time molecular composition of the aerosols is obtained by using a Direct Analysis in Real Time (DART) ionization source coupled to a high-resolution mass spectrometer. Aerosol mass spectra reveal that 3-methyltetrol sulfate ester can be detected as its anionic form (C5H11SO7-) via direct ionization in the negative ionization mode. Kinetic measurements reveal that the effective heterogeneous OH rate constant is measured to be 4.74±0.2×10-13 cm3 molecule−1 s−1 with a chemical lifetime against OH oxidation of 16.2±0.3 days, assuming an OH radical concentration of 1.5×106 molecules cm−3. Comparison of this lifetime with those against other aerosol removal processes, such as dry and wet deposition, suggests that 3-methyltetrol sulfate ester is likely to be chemically stable over atmospheric timescales. Aerosol mass spectra only show an increase in the intensity of bisulfate ion (HSO4-) after oxidation, suggesting the importance of fragmentation processes. Overall, potassium 3-methyltetrol sulfate ester likely decomposes to form volatile fragmentation products and aqueous-phase sulfate radial anion (SO4⚫-). SO4⚫- subsequently undergoes intermolecular hydrogen abstraction to form HSO4-. These processes appear to explain the compositional evolution of 3-methyltetrol sulfate ester during heterogeneous OH oxidation.

A sulfur(vi) fluoride exchange click chemistry approach towards main chain liquid crystal polymers bearing sulfate ester groups

Here we report a sulfur(vi) fluoride exchange click chemistry approach towards the synthesis of main chain liquid crystal polymers.

Heterogeneous OH Oxidation of Isoprene Epoxydiol-Derived Organosulfates: Kinetics, Chemistry and Formation of Inorganic Sulfate

Acid-catalyzed multiphase chemistry of epoxydiols formed from isoprene oxidation yields the most abundant organosulfates (i.e., methyltetrol sulfates) detected in atmospheric fine aerosols. This potentially determines the physicochemical properties of fine aerosols in isoprene-rich regions. However, chemical stability of these organosulfates remains unclear. As a result, we investigate the heterogeneous oxidation of aerosols consisting of potassium 3-methyltetrol sulfate ester (C5H11SO7K) by gas-phase hydroxyl (OH) radicals through studying the oxidation kinetics and reaction products at a relative humidity (RH) of 70.8 %. Real-time molecular composition of the aerosols is obtained by using a Direct Analysis in Real Time (DART) ionization source coupled to a high-resolution mass spectrometer. Aerosol mass spectra reveal that 3-methyltetrol sulfate ester can be detected as its anionic form (C5H11SO7−) via direct ionization in the negative ionization mode. Kinetic measurements reveal that the effective heterogeneous OH rate constant is measured to be 4.74 ± 0.2 × 10−13 cm3 molecule−1 s−1 with a chemical lifetime against OH oxidation of 16.2 ± 0.3 days. Comparison of this lifetime with those against other aerosol removal processes, such as dry and wet deposition, suggests that 3-methyltetrol sulfate ester is likely to be chemically stable over atmospheric timescales. Aerosol mass spectra only show an increase in the intensity of bisulfate ion (HSO4−) after oxidation, suggesting the absence of functionalization processes is likely attributable to the steric effect of substituted functional groups (e.g. methyl, alcohol and sulfate groups) on peroxy–peroxy radical reactions. Overall, potassium 3-methyltetrol sulfate ester likely decomposes to form volatile fragmentation products and aerosol-phase sulfate radial anion (SO4•−). SO4•− subsequently undergoes intermolecular hydrogen abstraction to form HSO4−. These processes appear to explain the compositional evolution of 3-methyltetrol sulfate ester during heterogeneous OH oxidation.