Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology
Living organisms use selenium mainly in the form of selenocysteine in the active site of oxidoreductases. Here, selenium’s unique chemistry is believed to modulate the reaction mechanism and enhance the catalytic efficiency of specific enzymes in ways not achievable with a sulfur-containing cysteine...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-12-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/29/1/120 |
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| author | Luisa B. Maia Biplab K. Maiti Isabel Moura José J. G. Moura |
| author_facet | Luisa B. Maia Biplab K. Maiti Isabel Moura José J. G. Moura |
| author_sort | Luisa B. Maia |
| collection | DOAJ |
| description | Living organisms use selenium mainly in the form of selenocysteine in the active site of oxidoreductases. Here, selenium’s unique chemistry is believed to modulate the reaction mechanism and enhance the catalytic efficiency of specific enzymes in ways not achievable with a sulfur-containing cysteine. However, despite the fact that selenium/sulfur have different physicochemical properties, several selenoproteins have fully functional cysteine-containing homologues and some organisms do not use selenocysteine at all. In this review, selected selenocysteine-containing proteins will be discussed to showcase both situations: (i) selenium as an obligatory element for the protein’s physiological function, and (ii) selenium presenting no clear advantage over sulfur (functional proteins with either selenium or sulfur). Selenium’s physiological roles in antioxidant defence (to maintain cellular redox status/hinder oxidative stress), hormone metabolism, DNA synthesis, and repair (maintain genetic stability) will be also highlighted, as well as selenium’s role in human health. Formate dehydrogenases, hydrogenases, glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases will be herein featured. |
| first_indexed | 2024-03-08T15:01:22Z |
| format | Article |
| id | doaj.art-73467c17996347709df29bc73ffa4b26 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-08T15:01:22Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-73467c17996347709df29bc73ffa4b262024-01-10T15:04:13ZengMDPI AGMolecules1420-30492023-12-0129112010.3390/molecules29010120Selenium—More than Just a Fortuitous Sulfur Substitute in Redox BiologyLuisa B. Maia0Biplab K. Maiti1Isabel Moura2José J. G. Moura3LAQV, REQUIMTE, Department of Chemistry, NOVA School of Science and Technology | NOVA FCT, 2829-516 Caparica, PortugalDepartment of Chemistry, School of Sciences, Cluster University of Jammu, Canal Road, Jammu 180001, IndiaLAQV, REQUIMTE, Department of Chemistry, NOVA School of Science and Technology | NOVA FCT, 2829-516 Caparica, PortugalLAQV, REQUIMTE, Department of Chemistry, NOVA School of Science and Technology | NOVA FCT, 2829-516 Caparica, PortugalLiving organisms use selenium mainly in the form of selenocysteine in the active site of oxidoreductases. Here, selenium’s unique chemistry is believed to modulate the reaction mechanism and enhance the catalytic efficiency of specific enzymes in ways not achievable with a sulfur-containing cysteine. However, despite the fact that selenium/sulfur have different physicochemical properties, several selenoproteins have fully functional cysteine-containing homologues and some organisms do not use selenocysteine at all. In this review, selected selenocysteine-containing proteins will be discussed to showcase both situations: (i) selenium as an obligatory element for the protein’s physiological function, and (ii) selenium presenting no clear advantage over sulfur (functional proteins with either selenium or sulfur). Selenium’s physiological roles in antioxidant defence (to maintain cellular redox status/hinder oxidative stress), hormone metabolism, DNA synthesis, and repair (maintain genetic stability) will be also highlighted, as well as selenium’s role in human health. Formate dehydrogenases, hydrogenases, glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases will be herein featured.https://www.mdpi.com/1420-3049/29/1/120selenium in biologyselenoproteinsformate dehydrogenaseshydrogenasesglutathione peroxidasesthioredoxin reductases |
| spellingShingle | Luisa B. Maia Biplab K. Maiti Isabel Moura José J. G. Moura Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology Molecules selenium in biology selenoproteins formate dehydrogenases hydrogenases glutathione peroxidases thioredoxin reductases |
| title | Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology |
| title_full | Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology |
| title_fullStr | Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology |
| title_full_unstemmed | Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology |
| title_short | Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology |
| title_sort | selenium more than just a fortuitous sulfur substitute in redox biology |
| topic | selenium in biology selenoproteins formate dehydrogenases hydrogenases glutathione peroxidases thioredoxin reductases |
| url | https://www.mdpi.com/1420-3049/29/1/120 |
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