Copper, which is a transition metal, serves essential functions as catalytic cofactors in a wide variety of critical cellular enzymes. A deficiency of the metal ion disrupts the functioning of a living system. It has been reported that the source of c...
Copper, which is a transition metal, serves essential functions as catalytic cofactors in a wide variety of critical cellular enzymes. A deficiency of the metal ion disrupts the functioning of a living system. It has been reported that the source of chelated copper is better than of free copper in terms of absorption in animals. Two amino acid components of proteins with a particular affinity for metal ions are histidine and cysteine. In addition to amino and carboxyl groups, histidine has an imidazole ring and cysteine a thiol group, which can participate in bonding to the copper ion. In this experiment, DNA containing multiple histidine codons was synthesized, oligomerized and ligated into a pET vector. The E. coli strain expressing the histidine-rich region had higher content of copper intracellualrly than the strain without expressing the histidine-rich region.