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Cytochrome c oxidase copper chaperone (COX17) is a small, essential mitochondrial protein that supplies copper ions for the assembly of cytochrome c oxidase (complex IV), the terminal enzyme of the mitochondrial electron transport chain[2][3][4]. COX17 binds copper ions in the cytosol and transfers them, via redox-regulated steps and interactions with other chaperones (such as SCO1, SCO2, COX11), to the mitochondrial intermembrane space and ultimately to the catalytic copper centers of cytochrome c oxidase[1][2][3]. Loss or knockdown of COX17 impairs cytochrome c oxidase function, impacting mitochondrial respiration and cellular energy production[3]. COX17 is not a structural subunit of the enzyme complex but is critical for its biogenesis. Increased activity and expression of COX17 have been implicated in certain cancers, making it a potential, though not yet clinically validated, therapeutic target in oncology[3].
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