Mechanism Of Sulfur Oxidation Research Articles

Triphenylene-Based 2D cMOFs: Unraveling the H2S Sensing Mechanism and Applications for a Real-Time Wireless Chemiresistive Sensor.

Two-dimensional conductive metal-organic frameworks (2D cMOFs) stand at the forefront of chemiresistive sensing innovations due to their high surface areas, distinctive morphologies, and substantial electronic conductivity. Particularly, 2D cMOFs crafted using 2,3,6,7,10,11-hexahydroxytriphenylene (HHTP) and 2,3,6,7,10,11-hexaiminotriphenylene (HITP) organic ligands have garnered a large amount of attention due to their designable active sites and proper conductive characteristics. Nevertheless, a deeper exploration into their sensing mechanisms is imperative for a comprehensive understanding of the intrinsic chemistry, which is crucial for the intricate design of specialized 2D cMOF chemiresistive sensors. In this study, we fabricate six M-HXTP (M = Co, Ni, and Cu; X = H and I) chemiresistive sensors, focusing on the application of hydrogen sulfide (H2S) detection. Among these, the 2D cMOFs incorporating Cu metal manifested a remarkably enhanced response to H2S. A combination of experimental and computational studies unveils the mechanisms of sulfur oxidation and Cu reduction, wherein distortion of the reduced MX4 cluster markedly amplifies the sensing response. Lastly, a real-time and portable wireless H2S sensing module has been demonstrated by using the Cu-HHTP composite material, highlighting the substantial practical significance and potential applicability.

Genome sequencing and metabolic network reconstruction of a novel sulfur-oxidizing bacterium Acidithiobacillus Ameehan.

Sulfur-oxidizing bacteria play a crucial role in various processes, including mine bioleaching, biodesulfurization, and treatment of sulfur-containing wastewater. Nevertheless, the pathway involved in sulfur oxidation is highly intricate, making it complete comprehension a formidable and protracted undertaking. The mechanisms of sulfur oxidation within the Acidithiobacillus genus, along with the process of energy production, remain areas that necessitate further research and elucidation. In this study, a novel strain of sulfur-oxidizing bacterium, Acidithiobacillus Ameehan, was isolated. Several physiological characteristics of the strain Ameehan were verified and its complete genome sequence was presented in the study. Besides, the first genome-scale metabolic network model (AMEE_WP1377) was reconstructed for Acidithiobacillus Ameehan to gain a comprehensive understanding of the metabolic capacity of the strain.The characteristics of Acidithiobacillus Ameehan included morphological size and an optimal growth temperature range of 37-45°C, as well as an optimal growth pH range of pH 2.0-8.0. The microbe was found to be capable of growth when sulfur and K2O6S4 were supplied as the energy source and electron donor for CO2 fixation. Conversely, it could not utilize Na2S2O3, FeS2, and FeSO4·7H2O as the energy source or electron donor for CO2 fixation, nor could it grow using glucose or yeast extract as a carbon source. Genome annotation revealed that the strain Ameehan possessed a series of sulfur oxidizing genes that enabled it to oxidize elemental sulfur or various reduced inorganic sulfur compounds (RISCs). In addition, the bacterium also possessed carbon fixing genes involved in the incomplete Calvin-Benson-Bassham (CBB) cycle. However, the bacterium lacked the ability to oxidize iron and fix nitrogen. By implementing a constraint-based flux analysis to predict cellular growth in the presence of 71 carbon sources, 88.7% agreement with experimental Biolog data was observed. Five sulfur oxidation pathways were discovered through model simulations. The optimal sulfur oxidation pathway had the highest ATP production rate of 14.81 mmol/gDW/h, NADH/NADPH production rate of 5.76 mmol/gDW/h, consumed 1.575 mmol/gDW/h of CO2, and 1.5 mmol/gDW/h of sulfur. Our findings provide a comprehensive outlook on the most effective cellular metabolic pathways implicated in sulfur oxidation within Acidithiobacillus Ameehan. It suggests that the OMP (outer-membrane proteins) and SQR enzymes (sulfide: quinone oxidoreductase) have a significant impact on the energy production efficiency of sulfur oxidation, which could have potential biotechnological applications.

Studying the mechanism and kinetics of fuel desulfurization using CexOy/NiOx piezo-catalysts as a new low-temperature method

In order to advance desulfurization technology, a new method for excellent oxidative desulfurization of fuel at room temperature will be of paramount importance. As a novel desulfurization method, we developed piezo-catalysts that do not require adding any oxidants and can be performed at room temperature. A microwave method was used to prepare CeO2/Ce2O3/NiOx nanocomposites. Model and real fuel desulfurization rates were examined as a function of synthesis parameters, such as microwave power and time, and operation conditions, such as pH and ultrasonic power. The results showed that CeO2/Ce2O3/NiOx nanocomposites demonstrated outstanding piezo-desulfurization at room temperature for both model and real fuels. Furthermore, CeO2/Ce2O3/NiOx nanocomposites exhibited remarkable reusability, maintaining 79% of their piezo-catalytic activity even after 17 repetitions for desulfurization of real fuel. An investigation of the mechanism of sulfur oxidation revealed that superoxide radicals and holes played a major role. Additionally, the kinetic study revealed that sulfur removal by piezo-catalyst follows a second-order reaction kinetic model.

Heterologous expression and biochemical comparison of two homologous SoxX proteins of endosymbiotic Candidatus Vesicomyosocius okutanii and free-living Hydrogenovibrio crunogenus from deep-sea environments

Candidatus Vesicomyosocius okutanii is a currently uncultured endosymbiotic bacterium of Phreagena okutanii, a clam that inhabits deep-sea vent environments. The genome of Ca. V. okutanii encodes a sulfur-oxidizing (Sox) enzyme complex, presumably generating biological energy for the host from inorganic sulfur compounds. Here, Ca. V. okutanii SoxX (VoSoxX), a mono-heme cytochrome c component of the Sox complex, was shown to be phylogenetically related to its homologous counterpart (HcSoxX) from a free-living deep-sea bacterium, Hydrogenovibrio crunogenus. Both proteins were heterologously expressed in Escherichia coli co-expressing cytochrome c maturation genes for comparative biochemical analysis. The VoSoxX recombinant had significantly lower thermal stability than HcSoxX, reflecting the difference in growth conditions of the source bacteria. The endosymbiont inhabits a mild intracellular environment, whereas the free-living bacterium dwells in a harsh environment. This study represents the first successful case of heterologous expression of genes from Ca. V. okutanii, allowing further biochemical studies of the molecular mechanism of sulfur oxidation in deep-sea environments.

Two pathways for thiosulfate oxidation in the alphaproteobacterial chemolithotroph Paracoccus thiocyanatus SST

Chemolithotrophic bacteria oxidize various sulfur species for energy and electrons, thereby operationalizing biogeochemical sulfur cycles in nature. The best-studied pathway of bacterial sulfur-chemolithotrophy involves direct oxidation of thiosulfate (S2O32−) to sulfate (SO42−) without any free intermediate. This pathway mediated by SoxXAYZBCD is apparently the exclusive mechanism of thiosulfate oxidation in facultatively chemolithotrophic alphaproteobacteria. Here we explore the molecular mechanisms of sulfur oxidation in the thiosulfate- and tetrathionate(S4O62−)-oxidizing alphaproteobacterium Paracoccus thiocyanatus SST, and compare them with the prototypical Sox process of Paracoccus pantotrophus. Our results reveal a unique case where an alphaproteobacterium has Sox as its secondary pathway of thiosulfate oxidation converting ∼10% of the thiosulfate supplied, whilst ∼90% of the substrate is oxidized via a pathway that produces tetrathionate as an intermediate. Sulfur oxidation kinetics of a deletion mutant showed that thiosulfate-to-tetrathionate conversion, in SST, is catalyzed by a thiosulfate dehydrogenase (TsdA) homolog that has far-higher substrate-affinity than the Sox system of this bacterium, which in turn is also less efficient than the P. pantotrophus Sox. Deletion of soxB abolished sulfate-formation from thiosulfate/tetrathionate, while thiosulfate-to-tetrathionate conversion remained unperturbed. Physiological studies revealed the involvement of glutathione in SST tetrathionate oxidation. However, zero impact of the insertional mutation of a thiol dehydrotransferase (thdT) homolog, together with the absence of sulfite as an intermediate, indicated that SST tetrathionate oxidation is mechanistically novel, and distinct from its betaproteobacterial counterpart mediated by glutathione, ThdT, SoxBCD and sulfite:acceptor oxidoreductase. The present findings highlight extensive functional diversification of sulfur-oxidizing enzymes across phylogenetically close, as well as distant, bacteria.

Insight Into Interactions of Thermoacidophilic Archaea With Elemental Sulfur: Biofilm Dynamics and EPS Analysis.

Biooxidation of reduced inorganic sulfur compounds (RISCs) by thermoacidophiles is of particular interest for the biomining industry and for environmental issues, e.g., formation of acid mine drainage (AMD). Up to now, interfacial interactions of acidophiles with elemental sulfur as well as the mechanisms of sulfur oxidation by acidophiles, especially thermoacidophiles, are not yet fully clear. This work focused on how a crenarchaeal isolate Acidianus sp. DSM 29099 interacts with elemental sulfur. Analysis by Confocal laser scanning microscopy (CLSM) and Atomic force microscopy (AFM) in combination with Epifluorescence microscopy (EFM) shows that biofilms on elemental sulfur are characterized by single colonies and a monolayer in first stage and later on 3-D structures with a diameter of up to 100 μm. The analysis of extracellular polymeric substances (EPS) by a non-destructive lectin approach (fluorescence lectin-barcoding analysis) using several fluorochromes shows that intial attachment was featured by footprints rich in biofilm cells that were embedded in an EPS matrix consisting of various glycoconjugates. Wet chemistry data indicate that carbohydrates, proteins, lipids and uronic acids are the main components. Attenuated reflectance (ATR)-Fourier transformation infrared spectroscopy (FTIR) and high-performance anion exchange chromatography with pulsed amperometric detection (HPAE-PAD) indicate glucose and mannose as the main monosaccharides in EPS polysaccharides. EPS composition as well as sugar types in EPS vary according to substrate (sulfur or tetrathionate) and lifestyle (biofilms and planktonic cells). This study provides information on the building blocks/make up as well as dynamics of biofilms of thermoacidophilic archaea in extremely acidic environments.

Metal-Assisted Oxo Atom Addition to an Fe(III) Thiolate.

Cysteinate oxygenation is intimately tied to the function of both cysteine dioxygenases (CDOs) and nitrile hydratases (NHases), and yet the mechanisms by which sulfurs are oxidized by these enzymes are unknown, in part because intermediates have yet to be observed. Herein, we report a five-coordinate bis-thiolate ligated Fe(III) complex, [FeIII(S2Me2N3(Pr,Pr))]+ (2), that reacts with oxo atom donors (PhIO, IBX-ester, and H2O2) to afford a rare example of a singly oxygenated sulfenate, [FeIII(η2-SMe2O)(SMe2)N3(Pr,Pr)]+ (5), resembling both a proposed intermediate in the CDO catalytic cycle and the essential NHase Fe-S(O)Cys114 proposed to be intimately involved in nitrile hydrolysis. Comparison of the reactivity of 2 with that of a more electron-rich, crystallographically characterized derivative, [FeIIIS2Me2NMeN2amide(Pr,Pr)]- (8), shows that oxo atom donor reactivity correlates with the metal ion's ability to bind exogenous ligands. Density functional theory calculations suggest that the mechanism of S-oxygenation does not proceed via direct attack at the thiolate sulfurs; the average spin-density on the thiolate sulfurs is approximately the same for 2 and 8, and Mulliken charges on the sulfurs of 8 are roughly twice those of 2, implying that 8 should be more susceptible to sulfur oxidation. Carboxamide-ligated 8 is shown to be unreactive towards oxo atom donors, in contrast to imine-ligated 2. Azide (N3-) is shown to inhibit sulfur oxidation with 2, and a green intermediate is observed, which then slowly converts to sulfenate-ligated 5. This suggests that the mechanism of sulfur oxidation involves initial coordination of the oxo atom donor to the metal ion. Whether the green intermediate is an oxo atom donor adduct, Fe-O═I-Ph, or an Fe(V)═O remains to be determined.

Interaction of Oxygen and Water with the (100) Surface of Pyrite: Mechanism of Sulfur Oxidation

We present a density-functional study of the adsorption and reactions of oxygen and water with the (100) surface of pyrite. We find that dissociative adsorption is energetically favorable for oxygen, forming ferryl-oxo, Fe(4+)═O(2-), species. These transform easily to ferric-hydroxy, Fe(3+)-OH(-), in the presence of coadsorbed water, and the latter fully covers the surface under room conditions. A mechanism for surface oxidation is identified, which involves successive reactions with molecular oxygen and water, and leads to the complete oxidation of a surface sulfur to SO4(2-). The crucial recurring process is the surface O(2-) and OH(-) species acting as proton acceptors for incoming water molecules. Using a recently proposed method, we examine the oxidation state changes of the surface ions and the electron flow during the adsorption and oxidation processes. The oxidation mechanism is consistent with isotopic labeling experiments, suggesting that the oxygens in SO4(2-) from gas-phase oxidation are derived from water.

Biochemistry and molecular biology of lithotrophic sulfur oxidation by taxonomically and ecologically diverse bacteria and archaea

Lithotrophic sulfur oxidation is an ancient metabolic process. Ecologically and taxonomically diverged prokaryotes have differential abilities to utilize different reduced sulfur compounds as lithotrophic substrates. Different phototrophic or chemotrophic species use different enzymes, pathways and mechanisms of electron transport and energy conservation for the oxidation of any given substrate. While the mechanisms of sulfur oxidation in obligately chemolithotrophic bacteria, predominantly belonging to Beta- (e.g. Thiobacillus) and Gammaproteobacteria (e.g. Thiomicrospira), are not well established, the Sox system is the central pathway in the facultative bacteria from Alphaproteobacteria (e.g. Paracoccus). Interestingly, photolithotrophs such as Rhodovulum belonging to Alphaproteobacteria also use the Sox system, whereas those from Chromatiaceae and Chlorobi use a truncated Sox complex alongside reverse-acting sulfate-reducing systems. Certain chemotrophic magnetotactic Alphaproteobacteria allegedly utilize such a combined mechanism. Sulfur-chemolithotrophic metabolism in Archaea, largely restricted to Sulfolobales, is distinct from those in Bacteria. Phylogenetic and biomolecular fossil data suggest that the ubiquity of sox genes could be due to horizontal transfer, and coupled sulfate reduction/sulfide oxidation pathways, originating in planktonic ancestors of Chromatiaceae or Chlorobi, could be ancestral to all sulfur-lithotrophic processes. However, the possibility that chemolithotrophy, originating in deep sea, is the actual ancestral form of sulfur oxidation cannot be ruled out.

Mechanism of sulfur oxidation in pyrite

The mechanism of sulfur oxidation in pyrite is a function of the rate and driving force for oxidation. New evidence is presented to show that, at moderate potentials, a sulfur-rich hydrophobic layer is formed. Under ordinary conditions, the sulfur layer is covered with a layer of iron oxides, hydroxides, sulfate or oxy-sulfide ions. Pyrite is hydrophilic under these conditions. In the presence of iron-chelating agents or iron sequestering ions, an iron layer might not form. Under these conditions, the sulfur layer is exposed, and the pyrite might become hydrophobic. Stronger oxidizing conditions decompose the sulfur layer, thereby making the surface hydrophilic.

Oxidation of elemental sulfur by an enzyme system of Thiobacillus thiooxidans

An enzyme present in the cell-free extracts of Thiobacillus thiooxidans oxidized elemental sulfur to thiosulfate in the presence of catalytic quantities of glutathione consuming 1 mole of O 2 for every mole of thiosulfate formed: ▪ The enzyme was partially purified and the purified preparation was free of sulfide-oxidizing activity and glutathione reductase (EC 1.6.4.2). The glutathione requirement was not replaced by other sulfhydryl compounds, oxidized glutathione or ascorbic acid. O 2 was also essential for the reaction and was not replaced by artificial electron acceptors. Catalase (EC 1.11.1.6) stimulated the sulfur oxidation after prolonged incubation period. Flavine nucleotides and KCN inhibited the reaction. A complex of elemental sulfur and glutathione was oxidized by the enzyme to thiosulfate. A possible mechanism of sulfur oxidation involving glutathione polysulfide as an intermediate is discussed.