Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase
Selenium-binding protein 1 (SELENBP1) was reported to act as a methanethiol oxidase (MTO) in humans, catalyzing the conversion of methanethiol to hydrogen peroxide, hydrogen sulfide and formaldehyde. Here, we identify copper ions as essential to this novel MTO activity. Site-directed mutagenesis of...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-09-01
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| Series: | Redox Biology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231723002082 |
| _version_ | 1797741466679771136 |
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| author | Thilo Magnus Philipp Leon Gernoth Andreas Will Maria Schwarz Verena Alexia Ohse Anna Patricia Kipp Holger Steinbrenner Lars-Oliver Klotz |
| author_facet | Thilo Magnus Philipp Leon Gernoth Andreas Will Maria Schwarz Verena Alexia Ohse Anna Patricia Kipp Holger Steinbrenner Lars-Oliver Klotz |
| author_sort | Thilo Magnus Philipp |
| collection | DOAJ |
| description | Selenium-binding protein 1 (SELENBP1) was reported to act as a methanethiol oxidase (MTO) in humans, catalyzing the conversion of methanethiol to hydrogen peroxide, hydrogen sulfide and formaldehyde. Here, we identify copper ions as essential to this novel MTO activity. Site-directed mutagenesis of putative copper-binding sites in human SELENBP1 produced as recombinant protein in E. coli resulted in loss of its enzymatic function. On the other hand, the eponymous binding of selenium (as selenite) was no requirement for MTO activity and only moderately increased SELENBP1-catalyzed oxidation of methanethiol. Furthermore, SEMO-1, the SELENBP1 ortholog recently identified in the nematode C. elegans, also requires copper ions, and MTO activity was enhanced or abrogated, respectively, if worms were grown in the presence of cupric chloride or of a Cu chelator. In addition to methanethiol, we identified novel substrates of SELENBP1 from the group of volatile sulfur compounds, ranging from ethanethiol to 1-pentanethiol as well as 2-propene-1-thiol. Gut microbiome-derived methanethiol as well as food-derived volatile sulfur compounds (VSCs) account for malodors that may contribute to extraoral halitosis in humans, if not metabolized properly. As SELENBP1 is particularly abundant in tissues exposed to VSCs, such as colon, liver, and lung, it appears to contribute to copper-dependent VSC degradation. |
| first_indexed | 2024-03-12T14:27:25Z |
| format | Article |
| id | doaj.art-7eba18ac8abf4f49b55b833947054c09 |
| institution | Directory Open Access Journal |
| issn | 2213-2317 |
| language | English |
| last_indexed | 2024-03-12T14:27:25Z |
| publishDate | 2023-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj.art-7eba18ac8abf4f49b55b833947054c092023-08-18T04:31:02ZengElsevierRedox Biology2213-23172023-09-0165102807Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidaseThilo Magnus Philipp0Leon Gernoth1Andreas Will2Maria Schwarz3Verena Alexia Ohse4Anna Patricia Kipp5Holger Steinbrenner6Lars-Oliver Klotz7Institute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Department of Nutritional Physiology, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Department of Nutritional Physiology, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, GermanyInstitute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Jena, Germany; Corresponding author. Institute of Nutritional Sciences, Nutrigenomics Section, Friedrich Schiller University Jena, Dornburger Strasse 29, D-07743, Jena, Germany.Selenium-binding protein 1 (SELENBP1) was reported to act as a methanethiol oxidase (MTO) in humans, catalyzing the conversion of methanethiol to hydrogen peroxide, hydrogen sulfide and formaldehyde. Here, we identify copper ions as essential to this novel MTO activity. Site-directed mutagenesis of putative copper-binding sites in human SELENBP1 produced as recombinant protein in E. coli resulted in loss of its enzymatic function. On the other hand, the eponymous binding of selenium (as selenite) was no requirement for MTO activity and only moderately increased SELENBP1-catalyzed oxidation of methanethiol. Furthermore, SEMO-1, the SELENBP1 ortholog recently identified in the nematode C. elegans, also requires copper ions, and MTO activity was enhanced or abrogated, respectively, if worms were grown in the presence of cupric chloride or of a Cu chelator. In addition to methanethiol, we identified novel substrates of SELENBP1 from the group of volatile sulfur compounds, ranging from ethanethiol to 1-pentanethiol as well as 2-propene-1-thiol. Gut microbiome-derived methanethiol as well as food-derived volatile sulfur compounds (VSCs) account for malodors that may contribute to extraoral halitosis in humans, if not metabolized properly. As SELENBP1 is particularly abundant in tissues exposed to VSCs, such as colon, liver, and lung, it appears to contribute to copper-dependent VSC degradation.http://www.sciencedirect.com/science/article/pii/S2213231723002082MTOMethanethiolVolatile sulfur compoundsVSCH2SH2O2 |
| spellingShingle | Thilo Magnus Philipp Leon Gernoth Andreas Will Maria Schwarz Verena Alexia Ohse Anna Patricia Kipp Holger Steinbrenner Lars-Oliver Klotz Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase Redox Biology MTO Methanethiol Volatile sulfur compounds VSC H2S H2O2 |
| title | Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase |
| title_full | Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase |
| title_fullStr | Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase |
| title_full_unstemmed | Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase |
| title_short | Selenium-binding protein 1 (SELENBP1) is a copper-dependent thiol oxidase |
| title_sort | selenium binding protein 1 selenbp1 is a copper dependent thiol oxidase |
| topic | MTO Methanethiol Volatile sulfur compounds VSC H2S H2O2 |
| url | http://www.sciencedirect.com/science/article/pii/S2213231723002082 |
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