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Effect of supersulfidation on rBSH enzymatic activity (A) MS/MS spectrum confirming supersulfidation at Cys2 in BSH following treatment with Na 2 S 4 and HPE-IAM (precursor m/z 962.9153, z = +2, ΔM = −0.56 ppm). B and y ions indicate peptide backbone fragment ions containing the N and C termini, respectively. “–H 2 O” denotes a dehydrated fragment ion. (B) Quantitative analysis of Cys2-containing peptide fragments following treatment with Na 2 S 4 and HPE-IAM. The stacked bar graph shows the proportions of the thiol- (Cys-S-AM-HPE), disulfide- (Cys–SS–AM-HPE), and trisulfide-labeled (Cys–SSS–AM-HPE) forms. (C) Reaction rate versus substrate concentration curves for L. reuteri BSH. Assays were performed as biological triplicates. Curves were fitted using non-linear regression analysis (Michaelis-Menten model) in GraphPad Prism using default parameters. (D) Time course of product formation in the L. reuteri bacterial assay. Cultured bacterial cells were treated with 1 mM <t>glycocholic</t> <t>acid.</t> Curves were fitted using non-linear regression analysis (One-phase association) in GraphPad Prism using default parameters. Data are expressed as means ± SEM. Statistical significance was assessed using two-way ANOVA with Holm-Šídák test. ∗∗ p < 0.01.
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Effect of supersulfidation on rBSH enzymatic activity (A) MS/MS spectrum confirming supersulfidation at Cys2 in BSH following treatment with Na 2 S 4 and HPE-IAM (precursor m/z 962.9153, z = +2, ΔM = −0.56 ppm). B and y ions indicate peptide backbone fragment ions containing the N and C termini, respectively. “–H 2 O” denotes a dehydrated fragment ion. (B) Quantitative analysis of Cys2-containing peptide fragments following treatment with Na 2 S 4 and HPE-IAM. The stacked bar graph shows the proportions of the thiol- (Cys-S-AM-HPE), disulfide- (Cys–SS–AM-HPE), and trisulfide-labeled (Cys–SSS–AM-HPE) forms. (C) Reaction rate versus substrate concentration curves for L. reuteri BSH. Assays were performed as biological triplicates. Curves were fitted using non-linear regression analysis (Michaelis-Menten model) in GraphPad Prism using default parameters. (D) Time course of product formation in the L. reuteri bacterial assay. Cultured bacterial cells were treated with 1 mM <t>glycocholic</t> <t>acid.</t> Curves were fitted using non-linear regression analysis (One-phase association) in GraphPad Prism using default parameters. Data are expressed as means ± SEM. Statistical significance was assessed using two-way ANOVA with Holm-Šídák test. ∗∗ p < 0.01.
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Effect of supersulfidation on rBSH enzymatic activity (A) MS/MS spectrum confirming supersulfidation at Cys2 in BSH following treatment with Na 2 S 4 and HPE-IAM (precursor m/z 962.9153, z = +2, ΔM = −0.56 ppm). B and y ions indicate peptide backbone fragment ions containing the N and C termini, respectively. “–H 2 O” denotes a dehydrated fragment ion. (B) Quantitative analysis of Cys2-containing peptide fragments following treatment with Na 2 S 4 and HPE-IAM. The stacked bar graph shows the proportions of the thiol- (Cys-S-AM-HPE), disulfide- (Cys–SS–AM-HPE), and trisulfide-labeled (Cys–SSS–AM-HPE) forms. (C) Reaction rate versus substrate concentration curves for L. reuteri BSH. Assays were performed as biological triplicates. Curves were fitted using non-linear regression analysis (Michaelis-Menten model) in GraphPad Prism using default parameters. (D) Time course of product formation in the L. reuteri bacterial assay. Cultured bacterial cells were treated with 1 mM <t>glycocholic</t> <t>acid.</t> Curves were fitted using non-linear regression analysis (One-phase association) in GraphPad Prism using default parameters. Data are expressed as means ± SEM. Statistical significance was assessed using two-way ANOVA with Holm-Šídák test. ∗∗ p < 0.01.
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Effect of supersulfidation on rBSH enzymatic activity (A) MS/MS spectrum confirming supersulfidation at Cys2 in BSH following treatment with Na 2 S 4 and HPE-IAM (precursor m/z 962.9153, z = +2, ΔM = −0.56 ppm). B and y ions indicate peptide backbone fragment ions containing the N and C termini, respectively. “–H 2 O” denotes a dehydrated fragment ion. (B) Quantitative analysis of Cys2-containing peptide fragments following treatment with Na 2 S 4 and HPE-IAM. The stacked bar graph shows the proportions of the thiol- (Cys-S-AM-HPE), disulfide- (Cys–SS–AM-HPE), and trisulfide-labeled (Cys–SSS–AM-HPE) forms. (C) Reaction rate versus substrate concentration curves for L. reuteri BSH. Assays were performed as biological triplicates. Curves were fitted using non-linear regression analysis (Michaelis-Menten model) in GraphPad Prism using default parameters. (D) Time course of product formation in the L. reuteri bacterial assay. Cultured bacterial cells were treated with 1 mM <t>glycocholic</t> <t>acid.</t> Curves were fitted using non-linear regression analysis (One-phase association) in GraphPad Prism using default parameters. Data are expressed as means ± SEM. Statistical significance was assessed using two-way ANOVA with Holm-Šídák test. ∗∗ p < 0.01.
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Effect of supersulfidation on rBSH enzymatic activity (A) MS/MS spectrum confirming supersulfidation at Cys2 in BSH following treatment with Na 2 S 4 and HPE-IAM (precursor m/z 962.9153, z = +2, ΔM = −0.56 ppm). B and y ions indicate peptide backbone fragment ions containing the N and C termini, respectively. “–H 2 O” denotes a dehydrated fragment ion. (B) Quantitative analysis of Cys2-containing peptide fragments following treatment with Na 2 S 4 and HPE-IAM. The stacked bar graph shows the proportions of the thiol- (Cys-S-AM-HPE), disulfide- (Cys–SS–AM-HPE), and trisulfide-labeled (Cys–SSS–AM-HPE) forms. (C) Reaction rate versus substrate concentration curves for L. reuteri BSH. Assays were performed as biological triplicates. Curves were fitted using non-linear regression analysis (Michaelis-Menten model) in GraphPad Prism using default parameters. (D) Time course of product formation in the L. reuteri bacterial assay. Cultured bacterial cells were treated with 1 mM glycocholic acid. Curves were fitted using non-linear regression analysis (One-phase association) in GraphPad Prism using default parameters. Data are expressed as means ± SEM. Statistical significance was assessed using two-way ANOVA with Holm-Šídák test. ∗∗ p < 0.01.

Journal: Redox Biology

Article Title: Formation of a reducing microenvironment and regulation of protein supersulfidation by gut microbial supersulfides

doi: 10.1016/j.redox.2026.104123

Figure Lengend Snippet: Effect of supersulfidation on rBSH enzymatic activity (A) MS/MS spectrum confirming supersulfidation at Cys2 in BSH following treatment with Na 2 S 4 and HPE-IAM (precursor m/z 962.9153, z = +2, ΔM = −0.56 ppm). B and y ions indicate peptide backbone fragment ions containing the N and C termini, respectively. “–H 2 O” denotes a dehydrated fragment ion. (B) Quantitative analysis of Cys2-containing peptide fragments following treatment with Na 2 S 4 and HPE-IAM. The stacked bar graph shows the proportions of the thiol- (Cys-S-AM-HPE), disulfide- (Cys–SS–AM-HPE), and trisulfide-labeled (Cys–SSS–AM-HPE) forms. (C) Reaction rate versus substrate concentration curves for L. reuteri BSH. Assays were performed as biological triplicates. Curves were fitted using non-linear regression analysis (Michaelis-Menten model) in GraphPad Prism using default parameters. (D) Time course of product formation in the L. reuteri bacterial assay. Cultured bacterial cells were treated with 1 mM glycocholic acid. Curves were fitted using non-linear regression analysis (One-phase association) in GraphPad Prism using default parameters. Data are expressed as means ± SEM. Statistical significance was assessed using two-way ANOVA with Holm-Šídák test. ∗∗ p < 0.01.

Article Snippet: A 10 mM solution of sodium glycocholate hydrate (Tokyo Chemical Industry Co., Ltd., Tokyo, Japan) was added to achieve a final concentration of 1 mM.

Techniques: Activity Assay, Tandem Mass Spectroscopy, Labeling, Concentration Assay, Cell Culture