COX5A Human

Cytochrome c oxidase, also known as Complex IV, is a crucial enzyme in the mitochondrial electron transport chain. It is responsible for the final step in the process of cellular respiration, where it facilitates the transfer of electrons from cytochrome c to molecular oxygen, resulting in the formation of water. This process is essential for the generation of ATP, the primary energy currency of the cell .

Cytochrome c oxidase is a large transmembrane protein complex composed of multiple subunits. Among these, subunit Va plays a significant role in the enzyme’s function and regulation. The human recombinant form of Cytochrome c oxidase subunit Va is a biotechnologically produced version of this protein, which is used in various research and clinical applications.

Cytochrome c oxidase subunit Va is one of the nuclear-encoded subunits of the enzyme complex. It is involved in the assembly and stability of the holoenzyme. The subunit interacts with other components of the complex to ensure proper electron transfer and proton pumping activities, which are critical for maintaining the electrochemical gradient across the inner mitochondrial membrane .

The enzyme complex contains several metal prosthetic sites, including heme groups and copper centers, which are essential for its catalytic activity. The cytochrome a3 and CuB form a binuclear center that is the site of oxygen reduction. This center accepts electrons from cytochrome c and facilitates the reduction of oxygen to water .

The human recombinant form of Cytochrome c oxidase subunit Va is typically produced using recombinant DNA technology. This involves the insertion of the gene encoding the subunit into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or yeast. The host cells are cultured under conditions that promote the expression of the recombinant protein, which is subsequently purified using various chromatographic techniques .

The human recombinant Cytochrome c oxidase subunit Va is widely used in biochemical and structural studies to understand the function and regulation of the enzyme complex. It is also employed in studies investigating the role of cytochrome c oxidase in various diseases, including neurodegenerative disorders and cancer .

Recent research has highlighted the importance of Cytochrome c oxidase subunit Va in the migration and invasion of non-small cell lung carcinoma (NSCLC) cells. Studies have shown that the expression of this subunit is significantly higher in tumorous areas and is associated with increased metastatic potential. Knockdown of Cytochrome c oxidase subunit Va using RNA interference techniques has been shown to reduce the migration and invasion of NSCLC cells, suggesting its potential as a therapeutic target .