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Metal Chaperones
Metal Chaperones also known as metallochaperones are soluble metal receptor proteins that transport metal ions to specific sites in an intracellular target protein. These enzymes facilitate metal transportation differently than metal buffers or chelators, which cause depletion of metals from separate cellular compartments resulting in the limitation in the biological interactions of metal ions. These metal chaperones are present to protect cells from potential cytotoxic reactions by maintaining a tight regulatory control over the cellular metal ion homeostasis so that the intracellular concentration of free metal ions such as zinc and copper is near zero.

During these processes, there are several components such as transporters, channels (voltage-gated calcium channels), and pumps (Calcium-ATPase) which allow these processes to take place. These components allow metal ions to transport across biological membranes. Also, they cause the endocytosis of the protein by allowing metal complexes to enter the cell and chaperones.

Copper Chaperones
All living systems require the use of copper. Cells have varying mechanisms that are required to deal with vital, however toxic trace elements. A recent discovery of copper chaperones is useful in attaining homeostatic mechanisms in which a protein-mediated, intracellular transportation of copper within target proteins takes place.

Copper chaperones are proteins that are essential in the cellular function of transporting copper to specific Cu proteins without causing damage or becoming trapped in the binding sites. These proteins are present within eukaryotes and prokaryotes and they prevent inappropriate interactions that take place within other cellular components. Once the copper metallochaperones are in contact with their associated cuproproteins, the copper ions are released. Copper supplies the mitochondria with CuA and intramembrane CuB sites of cytochrome oxidase. Furthermore, it also supplies secreted cuproproteins inside the trans-Golgi network and it is also needed to supply superoxide dismutase 1 (Sod1) within the cytosol.

Copper Delivery to the Mitochondria
Cytochrome oxidase(COX) is a superfamily of proteins, specifically an important terminal mitochondrial enzyme which requires the insertion of three copper ions into the following two subunits: a mononuclear copper site and a binuclear copper site. A monolayer nuclear site is present within the inner membranes and the binuclear copper site protrudes into the inner membrane space of the mitochondria. However, the mechanism of the insertion process of copper ions into the enzymes is unclear.

There are two proteins required for the cytochrome oxidase activity to have an effect on the utilization of copper are COX17 and SCO1. COX17 was originally discovered by Tzagoloff and co-workers.

Copper Delivery to the Golgi via ATX1 Pathway
When the gene ATX1(anti-oxidant) is present in yeast, it is able to protect itself from oxidative damage. An overproduction of ATX1 can provide this protection, however this may not be relevant since the activity seems to result from the stoichiometric, not catalytic consumption of superoxide by Cu-ATX1. Copper is transported to an intracellular copper transporter located in Golgi via ATX1. The copper transporter infuses the golgi lumen with metal which is inserted into the copper enzymes and these enzymes will eventually end up on the cell surface or extracellular matrix.

The transporters to which the copper is delivered by ATX1 are known as P-type ATPase which are driven via ATP-driven ion pumps.

Properties of Pentafluorophenol
Pentafluorophenol
 * Molecular formula: C6F5OH
 * Molecular weight: 184.06g/mol
 * Melting Point: 34-36°C
 * Boiling Point: 143°C
 * Appearance: White solid
 * Solubility: N/A

Pentafluorophenol

Organic Chemistry

Pentafluorophenol

Mechanism of Mo-Dependent Nitrogenase

Excitonic States in Photosystem II Reaction Center

Chemical Properties of Methanol and Butanol
$$ln(K_2/K_2)=\frac{\Delta H_{rxn}^o}{R} \bigl(\frac{1}{T_1}-\frac{1}{T_2}\bigr)$$