@Article{Su2017MnSODStudy,
  author    = {Jianmei Su and Zhou Li and Bei Liao and Yanhua Zhu and Xiaodi Zhang and Chunhong Wang and Jin He},
  journal   = {Journal of Thermal Analysis and Calorimetry Art},
  title     = {Microcalorimetric studyof the effect of manganese on the growth and metabolism in a heterogeneouslyexpressing manganese-dependent superoxide dismutase (Mn-SOD) strain},
  year      = {2017},
  pages     = {1407--1416},
  abstract  = {In bacteria, manganese (Mn) is best understood for its roles in protection against oxidative stress as a cofactor of manganese-dependent superoxide dismutase (Mn-SOD). There are four SOD enzymes, including two distinct Mn-SOD proteins (SodA1 and SodA2), with an approximately 53% amino sequence identity to each other, one Cu/Zn-SOD and one Fe-SOD in Bacillus thuringiensis. The specific activity of heterogeneously expressed SodA1 enzyme in Escherichia coli was 10,860 U mg−1, which was enhanced with the addition of elevated exogenous Mn(II) levels and reached the highest specific activity (14,519 U mg−1) at 80 μM Mn(II). However, neither the purified SodA1 enzyme nor the E. coli recombinant strain BL21-SOD could oxidize Mn(II) in vitro or in vivo. The growth of BL21-SOD strain was also increased by 2 mM Mn(II), and its intracellular accumulated Mn(II) level reached 41.5 μM. The obtained power–time curves from microcalorimetric assay demonstrated that Q peak of BL21-SOD cultivated with 2 mM Mn(II) was significantly increased, which was 3.55-fold and 3.85-fold higher than the parent strain BL21(DE3) and control strain BL21-pET, respectively, indicating that the exposure of Mn(II) and accompanying oxidative stress might induce and activate the overproduction of SodA1 to eliminate toxic O −2 .},
  doi       = {s10973-017-6282-8},
  url_paper = {https://link.springer.com/content/pdf/10.1007/s10973-017-6282-8.pdf}
}

{"_id":"ocHRGprNirwRzq7AW","bibbaseid":"su-li-liao-zhu-zhang-wang-he-microcalorimetricstudyoftheeffectofmanganeseonthegrowthandmetabolisminaheterogeneouslyexpressingmanganesedependentsuperoxidedismutasemnsodstrain-2017","author_short":["Su, J.","Li, Z.","Liao, B.","Zhu, Y.","Zhang, X.","Wang, C.","He, J."],"bibdata":{"bibtype":"article","type":"article","author":[{"firstnames":["Jianmei"],"propositions":[],"lastnames":["Su"],"suffixes":[]},{"firstnames":["Zhou"],"propositions":[],"lastnames":["Li"],"suffixes":[]},{"firstnames":["Bei"],"propositions":[],"lastnames":["Liao"],"suffixes":[]},{"firstnames":["Yanhua"],"propositions":[],"lastnames":["Zhu"],"suffixes":[]},{"firstnames":["Xiaodi"],"propositions":[],"lastnames":["Zhang"],"suffixes":[]},{"firstnames":["Chunhong"],"propositions":[],"lastnames":["Wang"],"suffixes":[]},{"firstnames":["Jin"],"propositions":[],"lastnames":["He"],"suffixes":[]}],"journal":"Journal of Thermal Analysis and Calorimetry Art","title":"Microcalorimetric studyof the effect of manganese on the growth and metabolism in a heterogeneouslyexpressing manganese-dependent superoxide dismutase (Mn-SOD) strain","year":"2017","pages":"1407–1416","abstract":"In bacteria, manganese (Mn) is best understood for its roles in protection against oxidative stress as a cofactor of manganese-dependent superoxide dismutase (Mn-SOD). There are four SOD enzymes, including two distinct Mn-SOD proteins (SodA1 and SodA2), with an approximately 53% amino sequence identity to each other, one Cu/Zn-SOD and one Fe-SOD in Bacillus thuringiensis. The specific activity of heterogeneously expressed SodA1 enzyme in Escherichia coli was 10,860 U mg−1, which was enhanced with the addition of elevated exogenous Mn(II) levels and reached the highest specific activity (14,519 U mg−1) at 80 μM Mn(II). However, neither the purified SodA1 enzyme nor the E. coli recombinant strain BL21-SOD could oxidize Mn(II) in vitro or in vivo. The growth of BL21-SOD strain was also increased by 2 mM Mn(II), and its intracellular accumulated Mn(II) level reached 41.5 μM. The obtained power–time curves from microcalorimetric assay demonstrated that Q peak of BL21-SOD cultivated with 2 mM Mn(II) was significantly increased, which was 3.55-fold and 3.85-fold higher than the parent strain BL21(DE3) and control strain BL21-pET, respectively, indicating that the exposure of Mn(II) and accompanying oxidative stress might induce and activate the overproduction of SodA1 to eliminate toxic O −2 .","doi":"s10973-017-6282-8","url_paper":"https://link.springer.com/content/pdf/10.1007/s10973-017-6282-8.pdf","bibtex":"@Article{Su2017MnSODStudy,\n author = {Jianmei Su and Zhou Li and Bei Liao and Yanhua Zhu and Xiaodi Zhang and Chunhong Wang and Jin He},\n journal = {Journal of Thermal Analysis and Calorimetry Art},\n title = {Microcalorimetric studyof the effect of manganese on the growth and metabolism in a heterogeneouslyexpressing manganese-dependent superoxide dismutase (Mn-SOD) strain},\n year = {2017},\n pages = {1407--1416},\n abstract = {In bacteria, manganese (Mn) is best understood for its roles in protection against oxidative stress as a cofactor of manganese-dependent superoxide dismutase (Mn-SOD). There are four SOD enzymes, including two distinct Mn-SOD proteins (SodA1 and SodA2), with an approximately 53% amino sequence identity to each other, one Cu/Zn-SOD and one Fe-SOD in Bacillus thuringiensis. The specific activity of heterogeneously expressed SodA1 enzyme in Escherichia coli was 10,860 U mg−1, which was enhanced with the addition of elevated exogenous Mn(II) levels and reached the highest specific activity (14,519 U mg−1) at 80 μM Mn(II). However, neither the purified SodA1 enzyme nor the E. coli recombinant strain BL21-SOD could oxidize Mn(II) in vitro or in vivo. The growth of BL21-SOD strain was also increased by 2 mM Mn(II), and its intracellular accumulated Mn(II) level reached 41.5 μM. The obtained power–time curves from microcalorimetric assay demonstrated that Q peak of BL21-SOD cultivated with 2 mM Mn(II) was significantly increased, which was 3.55-fold and 3.85-fold higher than the parent strain BL21(DE3) and control strain BL21-pET, respectively, indicating that the exposure of Mn(II) and accompanying oxidative stress might induce and activate the overproduction of SodA1 to eliminate toxic O −2 .},\n doi = {s10973-017-6282-8},\n url_paper = {https://link.springer.com/content/pdf/10.1007/s10973-017-6282-8.pdf}\n}\n\n\n\n\n\n\n","author_short":["Su, J.","Li, Z.","Liao, B.","Zhu, Y.","Zhang, X.","Wang, C.","He, J."],"key":"Su2017MnSODStudy","id":"Su2017MnSODStudy","bibbaseid":"su-li-liao-zhu-zhang-wang-he-microcalorimetricstudyoftheeffectofmanganeseonthegrowthandmetabolisminaheterogeneouslyexpressingmanganesedependentsuperoxidedismutasemnsodstrain-2017","role":"author","urls":{" paper":"https://link.springer.com/content/pdf/10.1007/s10973-017-6282-8.pdf"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bercher.net/bibtex/bibliography.bib","dataSources":["jNECE4duak4GHfRte","bPpsmYWjffAy6QHP5"],"keywords":[],"search_terms":["microcalorimetric","studyof","effect","manganese","growth","metabolism","heterogeneouslyexpressing","manganese","dependent","superoxide","dismutase","sod","strain","su","li","liao","zhu","zhang","wang","he"],"title":"Microcalorimetric studyof the effect of manganese on the growth and metabolism in a heterogeneouslyexpressing manganese-dependent superoxide dismutase (Mn-SOD) strain","year":2017}