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Selenium
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===Evolution in biology=== {{Main|Evolution of dietary antioxidants}} From about three billion years ago, [[prokaryotic]] selenoprotein families drove the evolution of the amino acid selenocysteine. Several selenoproteins are known in bacteria, archaea, and eukaryotes, invariably owing to the presence of selenocysteine,<ref name="glady">{{cite journal |title=Selenocysteine-containing proteins in mammals |journal=Journal of Biomedical Science |volume=6 |issue=3 |pages=151β160 |date=1999 |pmid=10343164 |doi=10.1007/BF02255899 |last1=Gladyshev |first1=Vadim N. |last2=Hatfield |first2=Dolph L.|url=https://digitalcommons.unl.edu/biochemgladyshev/77 }}</ref> Just as for mammals, selenoprotein protect unicellular organisms against oxidative damage. Selenoprotein families of GSH-Px and the deiodinases of eukaryotic cells seem to have a bacterial [[Phylogenetics|phylogenetic]] origin. The selenocysteine-containing form occurs in species as diverse as green algae, diatoms, sea urchins, fish, and chickens.<ref>{{cite journal |last=Stadtman |first=T. C. |title=Selenocysteine |journal=Annual Review of Biochemistry |volume=65 |pages=83β100 |date=1996 |issue=1 |pmid=8811175 |doi=10.1146/annurev.bi.65.070196.000503}}</ref> Trace elements involved in GSH-Px and superoxide dismutase enzymes activities, i.e., selenium, [[vanadium]], [[magnesium]], [[copper]], and [[zinc]], may have been lacking in some terrestrial mineral-deficient areas.<ref name="glady" /> Marine organisms retained and sometimes expanded their selenoproteomes, whereas the selenoproteomes of some terrestrial organisms were lowered or completely lost. These findings suggest that, with the exception of [[vertebrate]]s, aquatic life supports selenium use, whereas terrestrial habitats lead to lowered use of this trace element.<ref>{{cite journal |title=Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life |journal=Genome Biology |volume=8 |issue=9 |pages=R198 |date=2007 |pmid=17880704 |pmc=2375036 |doi=10.1186/gb-2007-8-9-r198 |last1=Lobanov |first1=Alexey V. |last2=Fomenko |first2=Dmitri E. |last3=Zhang |first3=Yan |last4=Sengupta |first4=Aniruddha |last5=Hatfield |first5=Dolph L. |last6=Gladyshev |first6=Vadim N. |display-authors=3 |doi-access=free }}</ref> Marine fishes and vertebrate thyroid glands have the highest concentration of selenium and iodine. From about 500 million years ago, freshwater and terrestrial plants slowly optimized the production of "new" endogenous antioxidants such as [[ascorbic acid]] (vitamin C), [[polyphenol]]s (including flavonoids), [[tocopherol]]s, etc. A few of these appeared in the last 50β200 million years in fruits and flowers of [[angiosperm]] plants. In fact, the angiosperms (the dominant type of plant today) and most of their antioxidant pigments evolved during the late [[Jurassic]] period.{{Citation needed|date=June 2016}} About 200 million years ago, new selenoproteins were developed as mammalian GSH-Px enzymes.<ref>{{cite journal |title=Reconsidering the evolution of eukaryotic selenoproteins: a novel nonmammalian family with scattered phylogenetic distribution |journal=EMBO Reports |volume=5 |issue=1 |pages=71β7 |date=2004 |pmid=14710190 |pmc=1298953 |doi=10.1038/sj.embor.7400036 |last1=Castellano |first1=Sergi |last2=Novoselov |first2=Sergey V. |last3=Kryukov |first3=Gregory V. |last4=Lescure |first4=Alain |last5=Blanco |first5=Enrique |last6=Krol |first6=Alain |last7=Gladyshev |first7=Vadim N. |last8=GuigΓ³ |first8=Roderic |display-authors=3}}</ref><ref>{{cite journal |title=The prokaryotic selenoproteome |journal=EMBO Reports |volume=5 |issue=5 |pages=538β43 |date=2004 |pmid=15105824 |pmc=1299047 |doi=10.1038/sj.embor.7400126 |last1=Kryukov |first1=Gregory V. |last2=Gladyshev |first2=Vadim N.}}</ref><ref>{{cite journal |title=Selenoprotein synthesis in archaea: identification of an mRNA element of ''Methanococcus jannaschii'' probably directing selenocysteine insertion |journal=Journal of Molecular Biology |volume=266 |issue=4 |pages=637β41 |date=1997 |pmid=9102456 |doi=10.1006/jmbi.1996.0812 |last1=Wilting |first1=R. |last2=Schorling |first2=S. |last3=Persson |first3=B. C. |last4=BΓΆck |first4=A.}}</ref><ref>{{cite journal |title=The microbial selenoproteome of the Sargasso Sea |journal=Genome Biology |volume=6 |issue=4 |pages=R37 |date=2005 |pmid=15833124 |pmc=1088965 |doi=10.1186/gb-2005-6-4-r37 |last1=Zhang |first1=Yan |last2=Fomenko |first2=Dmitri E. |last3=Gladyshev |first3=Vadim N. |doi-access=free }}</ref>
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