The pathway of sulfide oxidation to octasulfur globules in the cytoplasm of aerobic bacteria

2021 ◽  
Author(s):  
Tianqi Wang ◽  
Mingxue Ran ◽  
Xiaoju Li ◽  
Yequn Liu ◽  
Yufeng Xin ◽  
...  
Keyword(s):  
Heterotrophic Bacteria ◽  
Sulfide Oxidation ◽  
Aerobic Bacteria ◽  
Wild Type ◽  
Theoretical Support ◽  
Sulfur Globules ◽  
Sulfur Oxidizing ◽  
S Oxidation ◽  
Main Component ◽  
Bacterial Cytoplasm

Sulfur-oxidizing bacteria can oxidize hydrogen sulfide (H 2 S) to produce sulfur globules. Although the process is common, the pathway is unclear. In recombinant Escherichia coli and wild-type Corynebacterium vitaeruminis DSM20294 with SQR but no enzymes to oxidize zero valence sulfur, SQR oxidized H 2 S into short-chain inorganic polysulfide (H 2 S n , n≥2) and organic polysulfide (RS n H, n≥2), which reacted with each other to form long-chain GS n H (n≥2) and H 2 S n before producing octasulfur (S 8 ), the main component of elemental sulfur. GS n H also reacted with GSH to form GSnG (n≥2) and H 2 S; H 2 S was again oxidized by SQR. After GSH was depleted, SQR simply oxidized H 2 S to H 2 S n , which spontaneously generated S 8 . S 8 aggregated into sulfur globules in the cytoplasm. The results highlight the process of sulfide oxidation to S 8 globules in the bacterial cytoplasm and demonstrate the potential of using heterotrophic bacteria with SQR to convert toxic H 2 S into relatively benign S 8 globules. IMPORTANCE Our results support a process of H 2 S oxidation to produce octasulfur globules via SQR catalysis and spontaneous reactions in the bacterial cytoplasm. Since the process is an important event in geochemical cycling, a better understanding facilitates further studies and provides theoretical support for using heterotrophic bacteria with SQR to oxidize toxic H 2 S into sulfur globules for recovery.

scholarly journals Sulfur globule oxidation in green sulfur bacteria is dependent on the dissimilatory sulfite reductase system

Microbiology ◽  
2011 ◽  
Vol 157 (4) ◽  
pp. 1229-1239 ◽  
Author(s):  
Carina Holkenbrink ◽  
Santiago Ocón Barbas ◽  
Anders Mellerup ◽  
Hiroyo Otaki ◽  
Niels-Ulrik Frigaard
Keyword(s):  
Sulfide Oxidation ◽  
Green Sulfur Bacteria ◽  
Substrate Oxidation ◽  
Sulfite Reductase ◽  
Wild Type ◽  
Oxidation Rates ◽  
Dissimilatory Sulfite Reductase ◽  
Sulfur Bacteria ◽  
Sulfur Globules ◽  
Green Sulfur

Green sulfur bacteria (GSB) oxidize sulfide and thiosulfate to sulfate, with extracellular globules of elemental sulfur as an intermediate. Here we investigated which genes are involved in the formation and consumption of these sulfur globules in the green sulfur bacterium Chlorobaculum tepidum. We show that sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase (DSR) system. Deletion of dsrM/CT2244 or dsrT/CT2245, or the two dsrCABL clusters (CT0851–CT0854, CT2247–2250), abolished sulfur globule oxidation and prevented formation of sulfate from sulfide, whereas deletion of dsrU/CT2246 had no effect. The DSR system also seems to be involved in the formation of thiosulfate, because thiosulfate was released from wild-type cells during sulfide oxidation, but not from the dsr mutants. The dsr mutants incapable of complete substrate oxidation oxidized sulfide and thiosulfate about twice as fast as the wild-type, while having only slightly lower growth rates (70–80 % of wild-type). The increased oxidation rates seem to compensate for the incomplete substrate oxidation to satisfy the requirement for reducing equivalents during growth. A mutant in which two sulfide : quinone oxidoreductases (sqrD/CT0117 and sqrF/CT1087) were deleted exhibited a decreased sulfide oxidation rate (∼50 % of wild-type), yet formation and consumption of sulfur globules were not affected. The observation that mutants lacking the DSR system maintain efficient growth suggests that the DSR system is dispensable in environments with sufficiently high sulfide concentrations. Thus, the DSR system in GSB may have been acquired by horizontal gene transfer as a response to a need for enhanced substrate utilization in sulfide-limiting habitats.

scholarly journals The Heterotrophic Bacterium Cupriavidus pinatubonensis JMP134 Oxidizes Sulfide to Sulfate with Thiosulfate as a Key Intermediate

2020 ◽  
Vol 86 (22) ◽  
Author(s):  
Yufeng Xin ◽  
Rui Gao ◽  
Feifei Cui ◽  
Chuanjuan Lü ◽  
Honglei Liu ◽  
...  
Keyword(s):  
Gene Deletion ◽  
Heterotrophic Bacteria ◽  
Heterotrophic Bacterium ◽  
Sulfide Oxidation ◽  
Sulfur Oxidation ◽  
Content Type ◽  
Sulfide:Quinone Oxidoreductase ◽  
Main Pathway ◽  
Cell Assays ◽  
Sulfur Oxidizing

ABSTRACT Heterotrophic bacteria actively participate in the biogeochemical cycle of sulfur on Earth. The heterotrophic bacterium Cupriavidus pinatubonensis JMP134 contains several enzymes involved in sulfur oxidation, but how these enzymes work together to oxidize sulfide in the bacterium has not been studied. Using gene-deletion and whole-cell assays, we determined that the bacterium uses sulfide:quinone oxidoreductase to oxidize sulfide to polysulfide, which is further oxidized to sulfite by persulfide dioxygenase. Sulfite spontaneously reacts with polysulfide to produce thiosulfate. The sulfur-oxidizing (Sox) system oxidizes thiosulfate to sulfate. Flavocytochrome c sulfide dehydrogenase enhances thiosulfate oxidation by the Sox system but couples with the Sox system for sulfide oxidation to sulfate in the absence of sulfide:quinone oxidoreductase. Thus, C. pinatubonensis JMP134 contains a main pathway and a contingent pathway for sulfide oxidation. IMPORTANCE We establish a new pathway of sulfide oxidation with thiosulfate as a key intermediate in Cupriavidus pinatubonensis JMP134. The bacterium mainly oxidizes sulfide by using sulfide:quinone oxidoreductase, persulfide dioxygenase, and the Sox system with thiosulfate as a key intermediate. Although the purified and reconstituted Sox system oxidizes sulfide, its rate of sulfide oxidation in C. pinatubonensis JMP134 is too low to be physiologically relevant. The findings reveal how these sulfur-oxidizing enzymes participate in sulfide oxidation in a single bacterium.

scholarly journals Microbial Load on Paper/Polymer Currency and Coins

1970 ◽  
Vol 9 ◽  
pp. 105-109 ◽  
Author(s):  
Tista Prasai ◽  
Kayo Devi Yami ◽  
Dev Raj Joshi
Keyword(s):  
Key Words ◽  
Heterotrophic Bacteria ◽  
Science And Technology ◽  
Microbial Load ◽  
Disease Spread ◽  
Coliform Bacteria ◽  
Aerobic Bacteria ◽  
Contamination Level

Currency notes and coins serve as an agency of transmission of microorganisms since they are passed freely from hand to hand as a medium of exchange. A research, with an objective to explore the microbial load on Nepalese paper/ polymer currency notes and coins, was carried out at the Environment Laboratory of Nepal Academy of Science and Technology, Khumaltar from November 2006 to May 2007. All together 63 samples of paper/polymer notes and coins from different professionals of different places at Kathmandu were collected and analyzed for the presence of microorganisms. Among the total tested paper/ polymer and coin samples, 98.4% were found to have heterotrophic aerobic bacteria, 87.3% were contaminated with coliform bacteria and 79.4% showed presence of Staphylococci. Contamination level was found in increasing order of coins> polymer notes>paper notes. The presence of high microbial load on currency notes and coins indicate the potentials of such currencies for possible disease spread in the human communities. Key words: currency notes; coins; heterotrophic bacteria; Coliform bacteria; Staphylococci DOI: 10.3126/njst.v9i0.3173 Nepal Journal of Science and Technology 9 (2008) 105-109

A new strategy to improve ramie degumming based on removal of the xylan branched structure

2021 ◽  
pp. 004051752110449
Author(s):  
Huihui Wang ◽  
Tong Shu ◽  
Pandeng Li ◽  
Yun Bai ◽  
Mengxiong Xiang ◽  
...  
Keyword(s):  
Removal Rate ◽  
Natural Fibers ◽  
Green Manufacturing ◽  
Operating Conditions ◽  
Ramie Fiber ◽  
Wild Type ◽  
Acetyl Xylan Esterase ◽  
Degumming Process ◽  
Main Component ◽  
Engineered Strain

Ramie fiber is known as the “king of natural fibers,” and the key to its wide application is efficient and green manufacturing. Microbial degumming has gradually become a hot area of research due to its environmental protection and mild operating conditions. However, some gummy materials remain after microbial degumming. Xylan is the main component of residual gums; its acetylated branched chains create the space barrier that makes the removal of hemicellulose difficult during ramie degumming. An acetyl xylan esterase (AXE) was obtained from Bacillus pumilus and characterized to solve this problem. Its optimum temperature and pH were 35°C and 8.0, respectively, and it had good temperature and pH stability. These properties were consistent with the conditions of ramie degumming and they laid a foundation for the application of AXE in ramie degumming. Besides, an engineered strain with a high activity of AXE was constructed successfully on the basis of the wild-type degumming strain Pectobacterium carotovorum HG-49 and used for ramie degumming. The removal rate of hemicellulose and total gums by the engineered strain increased by 4.89% and 2.53%, respectively, compared with that of the wild-type strain. Moreover, the role of this AXE in ramie degumming was further proven by X-ray diffraction and scanning electron microscopy. This study showed that AXE played an important role in the removal of hemicellulose in the degumming process of ramie fibers, thus providing a promising degumming strategy for ramie and other bast fiber plants.

scholarly journals Cupriavidus necator H16 Uses Flavocytochrome c Sulfide Dehydrogenase To Oxidize Self-Produced and Added Sulfide

2017 ◽  
Vol 83 (22) ◽  
Author(s):  
Chuanjuan Lü ◽  
Yongzhen Xia ◽  
Daixi Liu ◽  
Rui Zhao ◽  
Rui Gao ◽  
...  
Keyword(s):  
Gas Phase ◽  
Heterotrophic Bacteria ◽  
Sulfide Oxidation ◽  
Cupriavidus Necator ◽  
Content Type ◽  
Sulfide:Quinone Oxidoreductase ◽  
Transport Chain ◽  
Genes Encoding ◽  
Cupriavidus Necator H16 ◽  
Chemolithotrophic Bacteria

ABSTRACT Production of sulfide (H2S, HS−, and S2−) by heterotrophic bacteria during aerobic growth is a common phenomenon. Some bacteria with sulfide:quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO) can oxidize self-produced sulfide to sulfite and thiosulfate, but other bacteria without these enzymes release sulfide into the medium, from which H2S can volatilize into the gas phase. Here, we report that Cupriavidus necator H16, with the fccA and fccB genes encoding flavocytochrome c sulfide dehydrogenases (FCSDs), also oxidized self-produced H2S. A mutant in which fccA and fccB were deleted accumulated and released H2S. When fccA and fccB were expressed in Pseudomonas aeruginosa strain Pa3K with deletions of its sqr and pdo genes, the recombinant rapidly oxidized sulfide to sulfane sulfur. When PDO was also cloned into the recombinant, the recombinant with both FCSD and PDO oxidized sulfide to sulfite and thiosulfate. Thus, the proposed pathway is similar to the pathway catalyzed by SQR and PDO, in which FCSD oxidizes sulfide to polysulfide, polysulfide spontaneously reacts with reduced glutathione (GSH) to produce glutathione persulfide (GSSH), and PDO oxidizes GSSH to sulfite, which chemically reacts with polysulfide to produce thiosulfate. About 20.6% of sequenced bacterial genomes contain SQR, and only 3.9% contain FCSD. This is not a surprise, since SQR is more efficient in conserving energy because it passes electrons from sulfide oxidation into the electron transport chain at the quinone level, while FCSD passes electrons to cytochrome c. The transport of electrons from the latter to O2 conserves less energy. FCSDs are grouped into three subgroups, well conserved at the taxonomic level. Thus, our data show the diversity in sulfide oxidation by heterotrophic bacteria. IMPORTANCE Heterotrophic bacteria with SQR and PDO can oxidize self-produced sulfide and do not release H2S into the gas phase. C. necator H16 has FCSD but not SQR, and it does not release H2S. We confirmed that the bacterium used FCSD for the oxidation of self-produced sulfide. The bacterium also oxidized added sulfide. The common presence of SQRs, FCSDs, and PDOs in heterotrophic bacteria suggests the significant role of heterotrophic bacteria in sulfide oxidation, participating in sulfur biogeochemical cycling. Further, FCSDs have been identified in anaerobic photosynthetic bacteria and chemolithotrophic bacteria, but their physiological roles are unknown. We showed that heterotrophic bacteria use FCSDs to oxidize self-produced sulfide and extraneous sulfide, and they may be used for H2S bioremediation.

scholarly journals The Xylanase Inhibitor TAXI-I Increases Plant Resistance to Botrytis cinerea by Inhibiting the BcXyn11a Xylanase Necrotizing Activity

Plants ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 601
Author(s):  
Silvio Tundo ◽  
Maria Chiara Paccanaro ◽  
Ibrahim Elmaghraby ◽  
Ilaria Moscetti ◽  
Renato D’Ovidio ◽  
...  
Keyword(s):  
Cell Wall ◽  
Botrytis Cinerea ◽  
Plant Cell Wall ◽  
Wild Type ◽  
Cell Wall Degrading Enzymes ◽  
Targeted Deletion ◽  
Plant Infection ◽  
Transgenic Lines ◽  
Xylanase Inhibitor ◽  
Main Component

During host plant infection, pathogens produce a wide array of cell wall degrading enzymes (CWDEs) to break the plant cell wall. Among CWDEs, xylanases are key enzymes in the degradation of xylan, the main component of hemicellulose. Targeted deletion experiments support the direct involvement of the xylanase BcXyn11a in the pathogenesis of Botrytis cinerea. Since the Triticum aestivum xylanase inhibitor-I (TAXI-I) has been shown to inhibit BcXyn11a, we verified if TAXI-I could be exploited to counteract B. cinerea infections. With this aim, we first produced Nicotiana tabacum plants transiently expressing TAXI-I, observing increased resistance to B. cinerea. Subsequently, we transformed Arabidopsis thaliana to express TAXI-I constitutively, and we obtained three transgenic lines exhibiting a variable amount of TAXI-I. The line with the higher level of TAXI-I showed increased resistance to B. cinerea and the absence of necrotic lesions when infiltrated with BcXyn11a. Finally, in a droplet application experiment on wild-type Arabidopsis leaves, TAXI-I prevented the necrotizing activity of BcXyn11a. These results would confirm that the contribution of BcXyn11a to virulence is due to its necrotizing rather than enzymatic activity. In conclusion, our experiments highlight the ability of the TAXI-I xylanase inhibitor to counteract B. cinerea infection presumably by preventing the necrotizing activity of BcXyn11a.

scholarly journals Two α(1-3) Glucan Synthases with Different Functions in Aspergillus fumigatus

2005 ◽  
Vol 71 (3) ◽  
pp. 1531-1538 ◽  
Author(s):  
A. Beauvais ◽  
D. Maubon ◽  
S. Park ◽  
W. Morelle ◽  
M. Tanguy ◽  
...  
Keyword(s):  
Cell Wall ◽  
Invasive Aspergillosis ◽  
Aspergillus Fumigatus ◽  
Molecular Mass ◽  
Mixed Infection ◽  
Cellular Localization ◽  
Amorphous Polymer ◽  
Wild Type ◽  
Main Component ◽  
Type Strains

ABSTRACT α(1-3) glucan is a main component of the Aspergillus fumigatus cell wall. In spite of its importance, synthesis of this amorphous polymer has not been investigated to date. Two genes in A. fumigatus, AGS1 and AGS2, are highly homologous to the AGS genes of Schizosaccharomyces pombe, which encode putative α(1-3) glucan synthases. The predicted Ags proteins of A. fumigatus have an estimated molecular mass of 270 kDa. AGS1 and AGS2 were disrupted in A. fumigatus. Both Δags mutants have similar altered hyphal morphologies and reduced conidiation levels. Only Δags1 presented a reduction in the α(1-3) glucan content of the cell wall. These results showed that Ags1p and Ags2p were functionally different. The cellular localization of the two proteins was in agreement with their different functions: Ags1p was localized at the periphery of the cell in connection with the cell wall, whereas Ags2p was intracellularly located. An original experimental model of invasive aspergillosis based on mixed infection and quantitative PCR was developed to analyze the virulence of A. fumigatus mutant and wild-type strains. Using this model, it was shown that the cell wall and morphogenesis defects of Δags1 and Δags2 were not associated with a reduction in virulence in either mutant. This result showed that a 50% reduction in the content of the cell wall α(1-3) glucan does not play a significant role in A. fumigatus pathogenicity.

Quantitative ecology of psychrophilic bacteria in an aquatic environment and characterization of heterotrophic bacteria from permanently cold sediments

1979 ◽  
Vol 25 (12) ◽  
pp. 1433-1442 ◽  
Author(s):  
L. G. Leduc ◽  
G. D. Ferroni
Keyword(s):  
Incubation Temperature ◽  
Heterotrophic Bacteria ◽  
Sulfate Reducing Bacteria ◽  
Gram Positive ◽  
Sulfate Reducing ◽  
Quantitative Ecology ◽  
Physiological Group ◽  
Sulfur Oxidizing ◽  
Reducing Bacteria

Aerobic heterotrophic bacteria, anaerobic heterotrophic bacteria, ammonifying bacteria, sulfur-oxidizing bacteria, and sulfate-reducing bacteria were quantitated in Fairbank Lake, an oligotrophic to mesotrophic lake with a permanently cold hypolimnion, as a function of depth in three seasons. Representatives of each physiological group were recovered at an incubation temperature of 2 °C and for all the physiological groups the 2 °C counts were usually higher than the 37 °C counts, although sulfate-reducing bacteria were not recoverable at an incubation temperature of 37 °C. In addition, the numbers of each physiological type were generally higher in the sediments than in the water column, except in the case of sulfate-reducing bacteria for which the counts were low and often below the detection limit. Aerobic heterotrophic bacteria usually outnumbered the other physiological groups surveyed, and winter minima were characteristic of some of the physiological groups. A relatively stable density of anaerobic heterotrophic bacteria, as a function of sediment depth, was observed when the incubation temperature was 2 °C. At 37 °C, these anaerobes were not detected, and this was true for sulfate-reducing bacteria at both temperatures.Heterotrophic bacterial isolates from the permanently cold sediments were examined with regard to Gram reaction, the obligate or facultative nature of anaerobes, ability to use ecologically important substrates, psychrophilic type, and temperature range for growth. Isolates recovered at 2 °C were predominantly Gram-negative bacilli, whereas isolates recovered at 37 °C were predominantly Gram-positive bacilli. The anaerobic isolates were mainly Gram-positive bacilli regardless of the isolation temperature, and most of those examined were obligately anaerobic. Many of the isolates tested were positive for gelatinase, chitinase, amylase, and lipase, but none was positive for cellulase. Most of the sediment isolates were facultatively psychrophilic and a considerable fraction of the 37 °C isolates were facultative psychrophiles.

scholarly journals Cytoplasmic Localization of Sulfide:Quinone Oxidoreductase and Persulfide Dioxygenase of Cupriavidus pinatubonensis JMP134

2017 ◽  
Vol 83 (23) ◽  
Author(s):  
Rui Gao ◽  
Honglei Liu ◽  
Luying Xun
Keyword(s):  
Organic Pollutants ◽  
Soluble Protein ◽  
Fluorescent Protein ◽  
Heterotrophic Bacteria ◽  
Sulfide Oxidation ◽  
Periplasmic Space ◽  
Microbial Oxidation ◽  
Content Type ◽  
Sulfide:Quinone Oxidoreductase ◽  
Chemolithotrophic Bacteria

ABSTRACT Heterotrophic bacteria have recently been reported to oxidize sulfide to sulfite and thiosulfate by using sulfide:quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO). In chemolithotrophic bacteria, both SQR and PDO have been reported to function in the periplasmic space, with SQR as a peripheral membrane protein whose C terminus inserts into the cytoplasmic membrane and PDO as a soluble protein. Cupriavidus pinatubonensis JMP134, best known for its ability to degrade 2,4-dichlorophenoxyacetic acid and other aromatic pollutants, has a gene cluster of sqr and pdo encoding C. pinatubonensis SQR (CpSQR) and CpPDO2. When cloned in Escherichia coli, the enzymes are functional. Here we investigated whether they function in the periplasmic space or in the cytoplasm in heterotrophic bacteria. By using sequence analysis, biochemical detection, and green fluorescent protein (GFP)/PhoA fusion proteins, we found that CpSQR was located on the cytoplasmic side of the membrane and CpPDO2 was a soluble protein in the cytoplasm with a tendency to be peripherally located near the membrane. The location proximity of these proteins near the membrane in the cytoplasm may facilitate sulfide oxidation in heterotrophic bacteria. The information may guide the use of heterotrophic bacteria in bioremediation of organic pollutants as well as H2S. IMPORTANCE Sulfide (H2S, HS−, and S2−), which is common in natural gas and wastewater, causes a serious malodor at low levels and is deadly at high levels. Microbial oxidation of sulfide is a valid bioremediation method, in which chemolithotrophic bacteria that use sulfide as the energy source are often used to remove sulfide. Heterotrophic bacteria with SQR and PDO have recently been reported to oxidize sulfide to sulfite and thiosulfate. Cupriavidus pinatubonensis JMP134 has been extensively characterized for its ability to degrade organic pollutants, and it also contains SQR and PDO. This paper shows the localization of SQR and PDO inside the cytoplasm in the vicinity of the membrane. The information may provide guidance for using heterotrophic bacteria in sulfide bioremediation.

scholarly journals The unusual cell wall of the Lyme disease spirochaete Borrelia burgdorferi is shaped by a tick sugar

2021 ◽  
Vol 6 (12) ◽  
pp. 1583-1592
Author(s):  
Tanner G. DeHart ◽  
Mara R. Kushelman ◽  
Sherry B. Hildreth ◽  
Richard F. Helm ◽  
Brandon L. Jutras
Keyword(s):  
Cell Wall ◽  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Cell Walls ◽  
Structural Strength ◽  
Cell Envelope ◽  
Wild Type ◽  
Tick Vector ◽  
Cell Wall Alteration ◽  
Main Component

AbstractPeptidoglycan—a mesh sac of glycans that are linked by peptides—is the main component of bacterial cell walls. Peptidoglycan provides structural strength, protects cells from osmotic pressure and contributes to shape. All bacterial glycans are repeating disaccharides of N-acetylglucosamine (GlcNAc) β-(1–4)-linked to N-acetylmuramic acid (MurNAc). Borrelia burgdorferi, the tick-borne Lyme disease pathogen, produces glycan chains in which MurNAc is occasionally replaced with an unknown sugar. Nuclear magnetic resonance, liquid chromatography–mass spectroscopy and genetic analyses show that B. burgdorferi produces glycans that contain GlcNAc–GlcNAc. This unusual disaccharide is chitobiose, a component of its chitinous tick vector. Mutant bacteria that are auxotrophic for chitobiose have altered morphology, reduced motility and cell envelope defects that probably result from producing peptidoglycan that is stiffer than that in wild-type bacteria. We propose that the peptidoglycan of B. burgdorferi probably evolved by adaptation to obligate parasitization of a tick vector, resulting in a biophysical cell-wall alteration to withstand the atypical torque associated with twisting motility.

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