Abstract
The CuA cofactor in cytochrome oxidase of mitochondria and many aerobic prokaryotes is a di-copper metal center that catalyzes one-electron transfer from cytochrome c to the oxygen-reducing active site. How the two copper ions are brought together for assembly of CuA is reported here. A thioredoxin-like disulfide reductase and two dedicated metal-lochaperones, one for Cu2+ and one for Cu1+, cooperate in this process. Copper insertion into cytochrome oxidase proceeds by a previously unknown mechanism.
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