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Significance Copper (Cu) is a cofactor of many enzymes in prokaryotes and eukaryotes, but Cu toxicity challenges cuproprotein biogenesis. To prevent Cu-induced damage while sustaining Cu supply for cuproproteins, cells possess sophisticated Cu transport and storage networks. P1B -type ATPases and Cu chaperones are central to these networks and preferentially bind Cu(I). However, under aerobic conditions, Cu exists primarily as Cu(II), and hence Cu(II) reduction is essential for Cu transport/storage. Eukaryotic organisms achieve this process via cell-surface exposed metalloreductases. For bacteria, it was generally assumed that the reducing environment of the cytoplasm would suffice to generate Cu(I). However, our findings now show that this dogma is incomplete, as we have identified a bacterial cupric reductase that reduces Cu(II) in the bacterial cytosol.

The cbb 3 -type cytochrome oxidase assembly factor CcoG is a widely distributed cupric reductase

The cbb ₃ -type cytochrome oxidase assembly factor CcoG is a widely distributed cupric reductase