ArticleJournal of bacteriology2012
The sulfur oxygenase reductase from the mesophilic bacterium Halothiobacillus neapolitanus is a highly active thermozyme.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Sulfur oxidation and implications for oxygen consumption in Base Mine Lake, the first pilot oil sands pit lake in the Athabasca oil sands region.Frontiers in microbiology · 2025Article
- pH and thiosulfate dependent microbial sulfur oxidation strategies across diverse environments.Frontiers in microbiology · 2024Article
- Chemoautotrophic production of gaseous hydrocarbons, bioplastics and osmolytes by a novel Halomonas species.Biotechnology for biofuels and bioproducts · 2023Article
- Cryo-electron structures of the extreme thermostable enzymes Sulfur Oxygenase Reductase and Lumazine Synthase.PloS one · 2022Article
- Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range.Applied microbiology and biotechnology · 2021Article
- Metaproteogenomic Profiling of Chemosynthetic Microbial Biofilms Reveals Metabolic Flexibility During Colonization of a Shallow-Water Gas Vent.Frontiers in microbiology · 2021Article
- The Microbial Composition in Circumneutral Thermal Springs from Chignahuapan, Puebla, Mexico Reveals the Presence of Particular Sulfur-Oxidizing Bacterial and Viral Communities.Microorganisms · 2020Article
- Crystallographic and cryogenic electron microscopic structures and enzymatic characterization of sulfur oxygenase reductase fromJournal of structural biology: X · 2020Article
- The Potential Role ofFrontiers in microbiology · 2019Article
- Biogeochemical Cycling by a Low-Diversity Microbial Community in Deep Groundwater.Frontiers in microbiology · 2018Article
- The Sulfur Oxygenase Reductase Activity Assay: Catalyzing a Reaction with Elemental Sulfur as Substrate at High Temperatures.Bio-protocol · 2017Article
- A Sulfur Oxygenase from the Haloalkaliphilic Bacterium Thioalkalivibrio paradoxus with Atypically Low Reductase Activity.Journal of bacteriology · 2017Article
- Sulfur Oxygenase Reductase (Sor) in the Moderately Thermoacidophilic Leaching Bacteria: Studies in Sulfobacillus thermosulfidooxidans and Acidithiobacillus caldus.Microorganisms · 2015Article
- Assessment of the stoichiometry and efficiency of CO2 fixation coupled to reduced sulfur oxidation.Frontiers in microbiology · 2015Article
- Metagenomic insights into S(0) precipitation in a terrestrial subsurface lithoautotrophic ecosystem.Frontiers in microbiology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A biochemical, biophysical, and phylogenetic study of the sulfur oxygenase reductase (SOR) from the mesophilic gammaproteobacterium Halothiobacillus neapolitanus (HnSOR) was performed in order to determine the structural and biochemical properties of the enzyme. SOR proteins from 14 predominantly chemolithoautotrophic bacterial and archaeal species are currently available in public databases. Sequence alignment and phylogenetic analysis showed that they form a coherent protein family. The HnSOR purified from Escherichia coli after heterologous gene expression had a temperature range of activity of 10 to 99°C with an optimum at 80°C (42 U/mg protein). Sulfite, thiosulfate, and hydrogen sulfide were formed at various stoichiometries in a range between pH 5.4 and 11 (optimum pH 8.4). Circular dichroism (CD) spectroscopy and dynamic light scattering showed that the HnSOR adopts secondary and quaternary structures similar to those of the 24-subunit enzyme from the hyperthermophile Acidianus ambivalens (AaSOR). The melting point of the HnSOR was ≈20°C lower than that of the AaSOR, when analyzed with CD-monitored thermal unfolding. Homology modeling showed that the secondary structure elements of single subunits are conserved. Subtle changes in the pores of the outer shell and increased flexibility might contribute to activity at low temperature. We concluded that the thermostability was the result of a rigid protein core together with the stabilizing effect of the 24-subunit hollow sphere.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.