Microcalorimetric study of the effect of manganese on the growth and metabolism in a heterogeneously expressing manganese-dependent superoxide dismutase (Mn-SOD) strain

Su, Jianmei; Li, Zhou; Liao, Bei; Zhu, Yanhua; Zhang, Xiaodi; Wang, Chunhong; He, Jin

doi:10.1007/s10973-017-6282-8

Cited by 6 publications

(2 citation statements)

References 60 publications

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“…Metal ions play important roles in molecular interactions and functions in biology: their thermodynamics studies have provided critical insights into the molecular mechanism [1][2][3][4][5]. Human immunodeficiency virus-1 reverse transcriptase (HIV-RT) possesses both nucleotide polymerization and ribonuclease H (RNH) activities, the latter of which degrades RNA of an RNA-DNA hybrid.…”

Section: Introductionmentioning

confidence: 99%

Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain

Oda

Zhang

Inaba

et al. 2018

J Therm Anal Calorim

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Metal-protein interactions are not necessarily tight in many transient biological processes, such as cellular signaling, enzyme regulation, and molecular recognition. Here, we analyzed the binding thermodynamics and characterized the structural effect of divalent metal ions, i.e. Mn 2+ , Zn 2+ , and Mg 2+ , to the isolated ribonuclease H (RNH) of human immunodeficiency virus (HIV) using isothermal titration calorimetry (ITC) and circular dichroism. The binding thermodynamics of Mg 2+ to RNH was determined using competition ITC experiments, and the binding affinity of Mg 2+ was found to be about 40-and 400-times lower than those of Mn 2+ and of Zn 2+ , respectively. The structural analysis showed that Mg 2+ binding had little effect on the thermal stability of RNH, while Zn 2+ and Mn 2+ binding increased the stability. The thermodynamic characteristics of RNH metal binding, compared to intact HIV reverse transcriptase, and a possible mechanism of conformational change induced upon metal ion binding, in correlation with the structure-function relationship, are discussed.

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Section: Introductionmentioning

confidence: 99%

Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain

Oda

Zhang

Inaba

et al. 2018

J Therm Anal Calorim

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“…However, when the concentration of MnSO 4 in the medium was higher than 500 µM, SOD activity significantly decreased ( p < 0.05) ( Figure 1 ). Previous studies have reported that Mn 2+ influences SOD expression in recombinant bacteria acting as a cofactor and changes SOD activity depending on Mn 2+ concentration [ 12 , 13 ]. A previous study also reported that addition of Mn 2+ to Mn 2+ -sufficient medium did not induce further synthesis of manganese superoxide dismutase (Mn-SOD) [ 14 ].…”

Section: Resultsmentioning

confidence: 99%

Antioxidant and Anti-Inflammatory Properties of Recombinant Bifidobacterium bifidum BGN4 Expressing Antioxidant Enzymes

Lin

Lim

et al. 2021

Microorganisms

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Bifidobacterium bifidum BGN4-SK (BGN4-SK), a recombinant strain which was constructed from B. bifidum BGN4 (BGN4) to produce superoxide dismutase (SOD) and catalase, was analyzed to determine its antioxidant and anti-inflammatory properties in vitro. Culture conditions were determined to maximize the SOD and catalase activities of BGN4-SK. The viability, intracellular radical oxygen species (ROS) levels, intracellular antioxidant enzyme activities, and pro-inflammatory cytokine levels were determined to evaluate the antioxidant and anti-inflammatory activities of BGN4-SK in human intestinal epithelial cells (HT-29) and murine macrophage cells (RAW 264.7). Antioxidant enzymes (SOD and catalase) were produced at the highest levels when BGN4-SK was cultured for 24 h in a medium containing 500 μM MnSO4 and 30 μM hematin, with glucose as the carbon source. The viability and intracellular antioxidant enzyme activities of H2O2-stimulated HT-29 treated with BGN4-SK were significantly higher (p < 0.05) than those of cells treated with BGN4. The intracellular ROS levels of H2O2-stimulated HT-29 cells treated with BGN4-SK were significantly lower (p < 0.05) than those of cells treated with BGN4. BGN4-SK more significantly suppressed the production of interleukin (IL)-6 (p < 0.05), tumor necrosis factor-α (p < 0.01), and IL-8 (p < 0.05) in lipopolysaccharide (LPS)-stimulated HT-29 and LPS-stimulated RAW 264.7 cells compared to BGN4. These results suggest that BGN4-SK may have enhanced antioxidant activities against oxidative stress in H2O2-stimulated HT-29 cells and enhanced anti-inflammatory activities in LPS-stimulated HT-29 and RAW 264.7 cells.

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