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Over three billion years ago, blue-green algae were the most primitive oxygenic photosynthetic organisms and are ancestors of multicellular eukaryotic algae.
Algae that contain the highest amount of antioxidant selenium, iodide, and peroxidase enzymes were the first living cells to produce poisonous oxygen in the atmosphere.
It has been suggested that algal cells required a protective antioxidant action, in which selenium and iodides, through peroxidase enzymes, have had this specific role.
Selenium, which acts synergistically with iodine, is a primitive mineral antioxidant, greatly present in the sea and prokaryotic cells, where it is an essential component of the family of glutathione peroxidase (GSH-Px) antioxidant enzymes; seaweeds accumulate high quantity of selenium and iodine.
From about three billion years ago, prokaryotic selenoprotein families drive selenocysteine evolution. Selenium is incorporated into several prokaryotic selenoprotein families in bacteria, archaea and eukaryotes as selenocysteine, where selenoprotein peroxiredoxins protect bacterial and eukaryotic cells against oxidative damage.
Selenoprotein families of GSH-Px and the deiodinases of eukaryotic cells seem to have a bacterial phylogenetic origin.
The selenocysteine-containing form occurs in species as diverse as green algae, diatoms, sea urchin, fish and chicken. Selenium enzymes are involved in utilization of the small reducing molecules glutathione and thioredoxin.
One family of selenium-containing molecules (the glutathione peroxidases) destroy peroxide and repair damaged peroxidized cell membranes, using glutathione.
Another selenium-containing enzyme in some plants and in animals (thioredoxin reductase) generates reduced thioredoxin, a dithiol that serves as an electron source for peroxidases and also the important reducing enzyme ribonucleotide reductase that makes DNA presursors from RNA precursors.
At about 500 Mya, plants and animals began to transfer from the sea to rivers and land, the environmental deficiency of marine mineral antioxidants (as selenium, iodine, etc.) was a challenge to the evolution of terrestrial life. Marine fishes and vertebrate thyroid glands have the highest concentration of selenium and iodine.
From about 500 Mya, freshwater and terrestrial plants slowly optimized the production of “new” endogenous antioxidants such as ascorbic acid (Vitamin C), polyphenols (including flavonoids), tocopherols, etc.
A few of these appeared more recently, in the last 50–200 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.
The deiodinase isoenzymes constitute another family of eukaryotic selenoproteins with identified enzyme function. Deiodinases are able to extract electrons from iodides, and iodides from iodothyronines.
They are, thus, involved in thyroid-hormone regulation, participating in the protection of thyrocytes from damage by H2O2
produced for thyroid-hormone biosynthesis.