ArticleExtremophiles : life under extreme conditions2014
Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase.
Article in Extremophiles : life under extreme conditions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 10 citations in OpenAlex.
- Utilization of Phenol as Carbon Source by the Thermoacidophilic ArchaeonFrontiers in microbiology · 2020Article
- Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications.World journal of microbiology & biotechnology · 2019Review
- Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus.Protoplasma · 2017Article
- Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.Extremophiles : life under extreme conditions · 2017Article
- Thermus thermophilus as source of thermozymes for biotechnological applications: homologous expression and biochemical characterization of an α-galactosidase.Microbial cell factories · 2017Article
- Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 fromArchaea (Vancouver, B.C.) · 2016Article
- Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27.Extremophiles : life under extreme conditions · 2014Article
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Authors and funding
6 authors at 3 institutions in 1 country.
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Abstract
Protein disulfide oxidoreductases (PDOs) are proteins involved in disulfide bond formation playing a crucial role in adaptation to extreme environment. This paper reports the functional and structural characterization of Sso1120, a PDO from the hyperthermophilic archaeon Sulfolobus solfataricus. The protein was expressed in Escherichia coli and purified to homogeneity. The functional characterization showed that the enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase that could be used in undiscovered pathways. The protein revealed a melting point of around 90 °C in CD spectroscopy-monitored thermal denaturation and high denaturant resistance. The X-ray crystallographic structure was solved at 1.80 Å resolution, showing differences with respect to other PDOs and an unexpected similarity with the N-terminal domain of the alkyl hydroperoxide reductase F component from Salmonella typhimurium. On the basis of the reported data and of bioinformatics and phylogenetic analyses, a possible involvement of this atypical PDO in a new antioxidant system of S. solfataricus has been proposed.
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