Petalitelle follows the reaction cycle of copper-zinc superoxide dismutase one step at a time and, at the close, sets the EU wording on copper beside it, word for word.
Open the MemoEvery cell contains oxygen molecules. When one of them picks up just a single electron, rather than the four it would take to end up as water, the result is the superoxide radical anion, written in formulas as O2•−. It lasts only a moment, carries a negative charge and reacts readily with the molecules around it.
Biochemists use the term oxidative stress when, over a longer stretch of time, the ratio between how fast reactive oxygen compounds form and how fast they are broken down tilts toward formation. So the phrase names no single substance; it names a lopsided ledger with two columns.
Among the first entries in the breakdown column is an enzyme with a copper atom at its active site: copper-zinc superoxide dismutase, usually shortened to SOD1 in the scientific literature. It makes an unusually clear illustration of what the authorized EU claim on copper refers to — which is why these pages revolve around it.
SOD1 is assembled from two matching subunits of roughly 150 amino acids apiece. Each subunit holds one copper ion and one zinc ion, sitting just a few tenths of a nanometer apart. The chemistry itself happens at the copper.
The copper ion can be present as Cu2+ or as Cu+. When a superoxide molecule meets the oxidized form, it gives up its surplus electron to the copper and exits the enzyme as ordinary oxygen. The copper, now reduced, passes that electron along to the next superoxide molecule, which combines with two protons to become hydrogen peroxide.
2 O2•− + 2 H+ → O2 + H2O2
At that point the copper is back to Cu2+, and the loop can start again. The enzyme is not consumed along the way. This exact sequence is the biochemical backdrop to the following claim:
Copper contributes to the protection of cells from oxidative stressEU-authorized wording · Regulation (EU) No 432/2012
The zinc ion never takes on electrons itself. It is linked to the copper through a shared histidine residue and keeps the protein loop that shapes the active site in its proper position. Without that structural anchor, the pocket around the copper would hold its shape less firmly.
The measured rate constant of SOD1 is on the order of 109 per mole per second. That is roughly as fast as molecules in a watery solution can bump into each other at all. The trick lies in positively charged amino acids at the mouth of the pocket, which steer the negatively charged superoxide straight toward the copper.
Core facts on copper, on where the enzyme is found and on the legal basis, laid out side by side.
Copper is an essential trace element, atomic number 29. An adult body holds only about 50 to 120 mg of it altogether. SOD1 needs the metal precisely because it moves so easily between two charge states.
The EU reference intake set by Regulation (EU) No 1169/2011 is 1 mg a day.
EU-authorized wording · Regulation (EU) No 432/2012
SOD1 turns up in nearly every cell type. Most of it is dissolved in the cell fluid, the cytosol. Smaller amounts are present in the nucleus and in the narrow gap between the two membranes of the mitochondria.
A related copper-containing form, SOD3, is anchored in tissue outside the cells.
The European Food Safety Authority (EFSA) examined the scientific data on copper. Working from that assessment, the European Commission entered the claim into the list in Regulation (EU) No 432/2012.
The wording is locked. It may not be expanded, nor may it be recast in other words with the same meaning.
A digital document with the reaction cycle broken into single steps, a data table on SOD1, the path copper follows into the enzyme and a sober reading of the EU claim.
One-time access · Digital information product
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