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Selenium
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Orientador(es)
Resumo(s)
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.
Descrição
FCT/MCTES is also acknowledged for the CEEC-Individual Program Contract (LBM). This work was also funded by DST–SERB for the CRG grant (file no CRG/2022/005673) and the Cluster University of Jammu for providing infrastructure facilities.
Publisher Copyright:
© 2023 by the authors.
Palavras-chave
formate dehydrogenases glutathione peroxidases human health hydrogenases iodothyronine deiodinases selenium in biology selenoproteins thioredoxin reductases Analytical Chemistry Chemistry (miscellaneous) Molecular Medicine Pharmaceutical Science Drug Discovery Physical and Theoretical Chemistry Organic Chemistry SDG 3 - Good Health and Well-being