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Copper Chaperones
Copper chaperones are essential in the safe and selective delivery of copper ions to proteins that require copper ions to function. Copper chaperones regulate the metabolism of copper ions and have various different motifs which help in the selective delivery of copper. Therefore, proteins that are copper dependent require unique copper chaperones which have similar structure/motif. Copper chaperones bind tightly to free copper ions (Cu+ and Cu2+) so that they do not oxidize other components of a cell. At low or high concentrations free copper ions are toxic when present inside a cell. The toxicity of copper ions causes the proteins, lipids, and nucleic acids that are present in the cytoplasm to bind with the free copper ions for detoxification purposes resulting is very small concentration of copper ions within a cell. Copper chaperones can have multiple functions with the primary one being the trafficking of copper ions. The second function is said to be linked with redox catalysis; CCS also known as the copper chaperone for superoxide dismutase is an example of a copper chaperone that undergoes disulfide oxidation as a secondary function.

Copper chaperones in Eukaryotes and Prokaryotes
The metabolism of copper is different in eukaryotes compared to prokaryotes due to the interaction with the mitochondria and endoplasmic reticulum that are present as well as the other components in the cytoplasm. The metabolism of copper chaperones in prokaryotic cells is much simpler because the cytoplasm in prokaryotes do not interact with the free copper ions.

There are many types of copper chaperones that exists in eukaryotes. Known examples are:


 * Atx1 and Atox1 copper chaperones
 * CCS
 * Cox 17
 * cox 11
 * Cox 19 and Cox 23
 * Sco1
 * Sco2