Generation of zero-valent sulfur from dissimilatory sulfate reduction in sulfate-reducing bacteria
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PROVIDER: PRJEB56267 | ENA |
REPOSITORIES: ENA
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Project description:We report a new DSR pathway that directly generates zero-valent sulfur (ZVS) in phylogenetically diverse SRB.
2023-04-27 | E-MTAB-12239 | biostudies-arrayexpress
Project description:Dissimilatory sulfate reduction (DSR) mediated by sulfate-reducing microorganisms (SRMs) plays a pivotal role in global sulfur, carbon, oxygen, and iron cycles since ~3.5 billion years ago. The canonical DSR pathway is believed to be sulfate reduction to sulfide. Herein, we report a new DSR pathway in phylogenetically diverse SRMs through which zero-valent sulfur (ZVS) is directly generated. We identified that approximately 8.9% of sulfate reduction was directed toward ZVS with S8 as a predominant product, and the ratio of sulfate-to-ZVS could be changed with SRMs’ growth conditions, particularly the medium salinity. Further coculturing experiments and metadata analyses revealed that DSR-derived ZVS supported the growth of various ZVS-metabolizing microorganisms, highlighting this new pathway as an essential component of the sulfur biogeochemical cycle
2023-04-28 | PXD040825 | Pride
Project description:Generation of zero-valent sulfur from dissimilatory sulfate reduction in sulfate-reducing bacteria
| PRJEB56466 | ENA
Project description:Production of zero valent sulfur from dissimilatory sulfate reduction in a methanogenic bioreactor
| PRJEB29929 | ENA
Project description:Bacteria isolated from diverse environments were found to sense blue light to regulate their biological functions. However, this ability of deep-sea bacteria has been studied rarely. In this study, we found serendipitously that blue light stimulated excess zero-valent sulfur (ZVS) production of E. flavus 21-3, which was isolated from the deep-sea cold seep and possessed a novel thiosulfate oxidation pathway. Its ZVS production responding to the blue light was mediated by a light-oxygen-voltage histidine kinase (LOV-1477), a diguanylate cyclase (DGC-2902), a PilZ protein (mPilZ-1753) and the key thiosulfate dehydrogenase (TsdA) in its thiosulfate oxidation pathway. Subsequently, the thiosulfohydrolase (SoxB-277) was found working with another SoxB (SoxB-285) and being as substitute for each other to generate ZVS. This study provided an example of deep-sea bacteria sensing blue light to regulate thiosulfate oxidation. Deep-sea blue light potentially helped these blue-light-sensing bacteria adapt harsh conditions by diversifying their biological processes.
2023-01-03 | PXD035435 | Pride
Project description:Molecular mechanism of zero valent iron-enhanced microbial azo reduction in Shewanella decolorationis S12
| PRJNA673394 | ENA
Project description:Nanoscale zero valent iron (nZVI) is used to remediate aquifers polluted by organochlorines or heavy metals and was also suggested to eliminate harmful algal blooms. nZVI can therefore affect microorganisms in the vicinity of the application area, including microalgae. However, studies on early transcriptomic effects of microalgae after exposure to nZVI are rare. Here, we described the early physiological and transcriptomic response of the freshwater ecological indicator green microalga, Raphidocelis subcapitata ATCC 22662, to 100 mg/L of reactive nZVI and non-reactive nano-magnetite (nFe3O4). The combined effect of shading and the release of total iron from nZVI posed a short-term inhibition effect leading to 15 % of deformed cells and cytosol leakage, while cells viability increased after 24 h. nZVI triggered a more pronounced transcriptomic response with (7380 differentially expressed genes [DEGs]) compared to nFe3O4 (4601 DEGs) after 1 h. nZVI, but not nFe3O4 increased the expression of genes function in DNA repair and replication, while deactivated carbohydrate-energy metabolisms, mitochondria signaling, and transmembrane ion transport. This study highlights an early fate assessment of algal cells under nZVI and nFe3O4 exposure using next-generation risk assessment methods and will serve as valuable information for safe and sustainable application of nZVI in water remediation.
2023-06-06 | GSE234088 | GEO
Project description:Pyrite formation upon Fe(III)-phosphate reduction by a microbial sulfur/sulfate-reducing consortium
| PRJEB29915 | ENA
Project description:BackgroundThe dissimilatory adenosine-5'-phosphosulfate (APS) reductase (cofactors flavin adenine dinucleotide, FAD, and two [4Fe-4S] centers) catalyzes the transformation of APS to sulfite and AMP in sulfate-reducing prokaryotes (SRP); in sulfur-oxidizing bacteria (SOB) it has been suggested to operate in the reverse direction. Recently, the three-dimensional structure of the Archaeoglobus fulgidus enzyme has been determined in different catalytically relevant states providing insights into its reaction cycle.Methodology/principal findingsFull-length AprBA sequences from 20 phylogenetically distinct SRP and SOB species were used for homology modeling. In general, the average accuracy of the calculated models was sufficiently good to allow a structural and functional comparison between the beta- and alpha-subunit structures (78.8-99.3% and 89.5-96.8% of the AprB and AprA main chain atoms, respectively, had root mean square deviations below 1 A with respect to the template structures). Besides their overall conformity, the SRP- and SOB-derived models revealed the existence of individual adaptations at the electron-transferring AprB protein surface presumably resulting from docking to different electron donor/acceptor proteins. These structural alterations correlated with the protein phylogeny (three major phylogenetic lineages: (1) SRP including LGT-affected Archaeoglobi and SOB of Apr lineage II, (2) crenarchaeal SRP Caldivirga and Pyrobaculum, and (3) SOB of the distinct Apr lineage I) and the presence of potential APS reductase-interacting redox complexes. The almost identical protein matrices surrounding both [4Fe-4S] clusters, the FAD cofactor, the active site channel and center within the AprB/A models of SRP and SOB point to a highly similar catalytic process of APS reduction/sulfite oxidation independent of the metabolism type the APS reductase is involved in and the species it has been originated from.ConclusionsBased on the comparative models, there are no significant structural differences between dissimilatory APS reductases from SRP and SOB; this might be indicative for a similar catalytic process of APS reduction/sulfite oxidation.
| S-EPMC2211403 | biostudies-literature
Project description:Mesophilic elemental sulfur reduction at neutral to acidic pH
| PRJEB50572 | ENA